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Institute of Cell Biology

Univ.-Prof. Dr.med.univ. Lukas A. Huber
Univ.-Prof. Dr.med.univ. Lukas A. Huber
Institute of Cell Biology

Innrain 80-82
6020 Innsbruck

Phone: +43 (0)512 9003 70170
Email: Lukas.A.Huber@i-med.ac.at
Website: https://cellbiology.i-med.ac.at/

Research Branch (ÖSTAT Classification)

106013, 106023, 106037, 106041, 106052, 301904, 302016, 302025, 302035, 302078, 302084

Keywords

cancer, Cell biology, genetic model organisms, metabolic signalling, organelle proteostasis, protein transport and sorting, proteomics, and rare diseases

Research Focus

Rare diseases
Cancer
Membrane Proteostasis and Signalling
Cell Differentiation
Signal Transduction and Proteomics

General Facts

At the Institute of Cell Biology, we are unraveling the molecular mechanisms that govern cellular function, from protein structure to the dysregulation underlying rare diseases. Our independent research groups are addressing fundamental questions in cell biology, structural biology and biochemistry by means of cutting-edge approaches, including high-resolution imaging, cryo-electron microscopy, genome editing and quantitative proteomics. We are using genetic models (yeast, mouse and human cells) to bridge the gap between molecular insights and disease mechanisms and are fostering translational collaborations with clinical and biotech partners. As a hub for innovation, we provide a vibrant, international research environment for Masters students, PhD students and postdoctoral fellows.

We are all funded by the FWF and represent major contributors to the MCBD (Molecular and Cellular Biology of Disease) PhD programme and the DOC82 (Cellular Basis of Diseases) doc.funds initiative, as well as to leading EU-funded projects and global academic partnerships. By bringing together basic research and clinical applications, we are driving discoveries that elucidate cellular health and disease.

Research

The Huber laboratory:  unlocking the secrets of lysosomal mTOR signalling

Our story begins in 2003 when we transformed our understanding of cellular signalling by identifying the LAMTOR/Ragulator complex and showing how the p14-MP1 scaffold anchors MAPK signalling to endosomes, a crucial step in regulating cell growth and survival (Teis et al., Dev Cell 2003). In 2007, we linked this complex to human disease, identifying p14 deficiency as the cause of a devastating primary immunodeficiency (Bohn et al, Nat Med 2007). This was the first indication that LAMTOR was more than a mere signalling hub – it is a lifeline. The plot thickened in 2015 when, in collaboration with Giulio Superti-Furga, we discovered SLC38A9, the long-sought amino-acid sensor that allows mTORC1 to ‘taste’ nutrients in lysosomes (Rebsamen et al, Nature 2015). Suddenly the pieces fell into place – LAMTOR was not only a scaffold, it was the control centre of metabolic decision-making. The structural revolution enabled us in 2017 to capture the first crystal structure of LAMTOR/Ragulator with Rag GTPases, revealing how this molecular machine aligns mTORC1 signalling on lysosomes (Araujo et al., Science 2017). In the same year, we showed that LAMTOR also controls lysosomal positioning, acting as a brake on endosomal motility (Filipek et al., JCB 2017). The story took an exciting turn in 2020, when – together with Jim Hurley and Andrea Ballabio – we linked LAMTOR dysfunction to the Birt-Hogg-Dubé syndrome, showing how faulty mTORC1 regulation drives this rare disease (Napolitano et al., Nature 2020). Finally, in 2023, we unveiled the megacomplex – a gigantic assembly of mTORC1, TFEB, Ragulator and Rags – painting a complete picture of how lysosomes orchestrate cellular metabolism (Cui et al., Nature 2023). From cancer to immune disorders, the LAMTOR complex is at the heart of disease and we are gradually unlocking its secrets, one discovery at a time.

The LAMTOR/Ragulator complex © modified from Araujo et al, Science 2017

The Vogel laboratory: intracellular cargo transport in congenital intestinal diseases

We are focusing on congenital intestinal and liver diseases, which are often caused by mutations in genes that are essential for correct intestinal-epithelial polarization. For example, we have identified mutations in MYO5B and STX3 in microvillus inclusion disease: both genes are essential for the polarized apical cargo transport of transmembrane transporters (Vogel GF et al., JCB, 2015; Vogel GF et al., JCI Insight, 2017; Szabó L et al., Traffic, 2024). We are now turning our attention to myo5b-associated cholestatic liver disease and myo5b-independent apical transport in intestinal epithelial cells.

We recently described the first case of a congenital enteropathy due to mutations in ezrin (manuscript in press), a protein involved in the establishment of proper apical polarity and plasma membrane composition in epithelial cells. We are also addressing the role of the retriever complex and the poorly characterized protein TM9SF4 in polarized plasma membrane cargo trafficking in epithelial cells.

Current understanding of proteins involved in intracellular polarized trafficking in epithelial cells (A, B) and phenotypes from mutations (C). © modiefied from Szabo et al, Traffic, 2024

The Vietor laboratory: regulatory mechanisms of cell differentiation

Our group is interested in the roles of the TPA-induced sequence-7 (TIS7, also known as IFRD1) protein and its orthologue SKMc15 (IFRD2). We have shown that they are involved in the regulation of the differentiation of neurons, enterocytes, myocytes and adipocytes and that TIS7 is a transcriptional co-regulator (Lammirato et al., BMC Biol, 2016). We have generated TIS7 and SKMc15 double knockout (dKO) mice and used them to identify a regulatory role for TIS7 in adipocyte differentiation and in resistance to high-fat diet (Vietor et al. eLife, 2023). As dKO mice are substantially leaner, we propose that TIS7 and SKMc15 are involved in physiological adipocyte differentiation. However, our mouse model does not enable us to distinguish between a systemic and a tissue-specific role of the two genes. We are thus generating constitutive knockout mouse models that specifically lack the expression of these genes in either the small intestine or adipocyte tissues. We are also establishing mouse organoid technology to limit the use of experimental animals and to permit us to study the role of the two genes more closely.

TIS7 and SKMc15 regulate number and size of lipid droplets. Electron micrographs of MEF cells isolated from wild-type (left) and TIS7 SKMc15 double-knockout (right) mice after 8 days of the adipocyte differentiation protocol. © Michael W. Hess
TIS7 and SKMc15 regulate number and size of lipid droplets. Electron micrographs of MEF cells isolated from wild-type (left) and TIS7 SKMc15 double-knockout (right) mice after 8 days of the adipocyte differentiation protocol. © Michael W. Hess

The Schmidt laboratory: regulation of cellular lipid homeostasis

Sphingolipids are an essential class of lipids. Their biosynthesis is initiated at the endoplasmic reticulum by the enzyme serine-palmitoyl-coenzyme A transferase (SPT), the activity of which is controlled by the evolutionarily conserved ORMDL protein family. ORMDL proteins associate with and thereby inhibit SPT. Genetic mutations that affect the interaction are of high pathological relevance and uncontrolled synthesis of sphingolipid precursors causes severe neurodegenerative phenotypes, including amyotrophic lateral sclerosis and frontotemporal dementia. We are studying the regulation of SPT in the light of differences between ORMDL paralogs.

Regulation of serine palmitoyl-CoA transferase (SPT) activity by ORMDL family proteins in yeast cells (EGAD, endosome- and Golgi-associated degradation; 3A, non-phosphorylatable Orm2 mutant; 3D, phospho-mimetic Orm2 mutant). © Oliver Schmidt

The Valovka laboratory: molecular basis of rare genetic disorders

Rare diseases are often the result of harmful genetic variants but the precise molecular effects of these variants remain poorly understood. Our group is working to identify the genetic culprits behind the disorders and to uncover how they hijack cellular processes to cause disease. In close collaboration with the Department of Paediatrics and Adolescent Medicine at MUI (Andreas Janecke and Thomas Müller), we have identified and are studying unique pathogenic mutations in various genes, including PCNT, SLC5A1, PCSK1, RIPK1 and UNC45A.

The osteo-oto-hepato-enteric (O2HE) syndrome is an autosomal recessive disease ascribed to loss-of-function mutations in the Unc-45 myosin chaperone A (UNC45A) gene. The clinical spectrum includes bone fragility, hearing loss, cholestasis, neurological symptoms and life-threatening diarrhoea associated with microvillus inclusion disease (MVID)-like enteropathy. We are trying to understand how a deficiency of or specific mutations in UNC45A affect the complex molecular mechanism of this severe neonatal disease. We have described a novel missense variant of UNC45A, c.710T>C, with unique pathogenicity caused by altered

chaperone-myosin interactions rather than a complete loss of chaperone function. The findings indicate the possibility of treatment and may guide the development of targeted therapies.

We are also screening natural anti-inflammatory compounds. In collaboration with the Austrian Drug Screening Institute (ADSI), we have developed a screening platform to identify and evaluate bioactive compounds in natural extracts. We were able to show the anti-inflammatory and cytoprotective polypharmacology of the complex herbal medicine Canephron N® (Bionorica SE) and to identify its mechanism of action.

Microvillus inclusion disease (MVID)-like enteropathy is associated with the UNC45A c.710T>C (p.Leu237Pro) variant identified in a patient with osteo-oto-hepato-enteric (O2HE) syndrome. (Left) Electron micrograph of CaCo2 UNC45A c.710T>C mutant cells showing ectopic microvillus arrays. (Right) Ribbon representation of the AlphaFold-predicted human UNC45A protein structure, showing in red the changes in vibrational entropy (ΔΔSVib) between the wild-type and mutant proteins (modified from Waich et al., JCI Insight. 2025; https://doi.org/10.1172/jci.insight.185508) © modified from Waich et al., JCI Insight. 2025

The Araujo laboratory: lysosomal signaling complexes – coordinating organelle function with cellular homeostasis

Lysosomes are membrane-bound organelles with several functions, from protein degradation to the control of cellular metabolism. Due to their importance for proteostasis and signaling, cells have developed mechanisms to control lysosomal numbers, size, movement, degradative capacity, interaction with other organelles and even lysophagy. Dysfunction is linked to numerous diseases, including lysosomal storage disorders, neurodegeneration, metabolic conditions and cancer.

Lysosomal adaptation. Lysosomal function is regulated by a plethora of proteins that control intrinsic lysosomal properties such us pH, organelle size and interaction with other organelles. Figure modified from de Araujo et al., Traffic 2020. © Figure modified from de Araujo et al., Traffic 2020

One of the key signaling complexes in the lysosomal membrane is mTORC1. Building on the knowledge from numerous laboratories over more than 30 years of research on this kinase, we are investigating how mTORC1 signaling components bind and coordinate their functions with other lysosomal proteins/complexes to maintain cellular homeostasis. We are also exploring how dysfunction of these processes contributes to disease. We use a combination of classical biochemical and cell biology methods, genome editing, live-cell imaging and super-resolution microscopy.

The Stasyk laboratory: molecular architecture of native lysosomal protein assemblies

Lysosomes are intracellular signaling platforms that govern cell growth, division and differentiation. Although our knowledge of the molecular mechanisms of the sensing of essential nutrients has advanced significantly, we still lack information on the interplay between the numerous components of sensing and signaling machineries. The LAMTOR/Ragulator complex is a crucial regulator of lysosomal mTORC1, MAPK and AMPK signaling. Via the BORC complex, LAMTOR also coordinates lysosome biogenesis. The existence of distinct LAMTOR complexes on lysosomes raises questions on how anabolic and catabolic signaling, lysosomal biogenesis and positioning are coordinated.

We are aiming to identify all LAMTOR- and BORC-associated protein assemblies on intact lysosomes and to obtain evidence for direct and endogenous protein-protein interactions. We are applying cross-linking mass spectrometry (XL-MS) in combination with subcellular fractionation to understand the molecular architectures of the protein complexes under different physiological conditions. Our approach captures native endogenous protein interactions using a chemical cross-linker that is reactive towards specific amino-acid side chains that are in close spatial proximity.

Caption: Native affinity-purified LAMTOR-interacting protein complexes, visualization using String V11.5. ©Taras Stasyk

Pictures

Selected Publications

The Huber Laboratory: Lysosomal mTOR Signalling – The Crossroads between Signal Transduction and Endosomal Biogenesis

1: Vogel GF, Klee KMC, Demir AM, Garczarczyk-Asim D, Hess MW, Huber LA, Mülller T, Janecke AR. Congenital enteropathy caused by ezrin deficiency. Hum Genet.2025 Mar 26. doi: 10.1007/s00439-025-02738-w. Epub ahead of print. PMID:40137958.

2: Waich S, Kreidl K, Vodopiutz J, Demir AM, Pollio AR, Dostál V, Pfaller K, Parlato M, Cerf-Bensussan N, Adam R, Vogel GF, Uhlig HH, Ruemmele FM, Müller T, Hess MW, Janecke AR, Huber LA, Valovka T. Altered chaperone-nonmuscle myosin II interactions drive pathogenicity of the UNC45A c.710T>C variant in osteo-oto-hepato-enteric syndrome. JCI Insight. 2025 Mar 24;10(6):e185508. doi:

10.1172/jci.insight.185508. PMID: 40125554.

3: Liebscher G, Vujic N, Schreiber R, Heine M, Krebiehl C, Duta-Mare M, Lamberti G, de Smet CH, Hess MW, Eichmann TO, Hölzl S, Scheja L, Heeren J, Kratky D, Huber LA. The lysosomal LAMTOR / Ragulator complex is essential for nutrient homeostasis in brown adipose tissue. Mol Metab. 2023 May;71:101705. doi: 10.1016/j.molmet.2023.101705. Epub 2023 Mar 11. PMID: 36907508; PMCID:

PMC10074977.

4: Cui Z, Napolitano G, de Araujo MEG, Esposito A, Monfregola J, Huber LA, Ballabio A, Hurley JH. Structure of the lysosomal mTORC1-TFEB-Rag-Ragulator megacomplex. Nature. 2023 Feb;614(7948):572-579. doi: 10.1038/s41586-022-05652-7. Epub 2023 Jan 25. PMID: 36697823; PMCID: PMC9931586.

5: Vietor I, Cikes D, Piironen K, Vasakou T, Heimdörfer D, Gstir R, Erlacher MD,Tancevski I, Eller P, Demetz E, Hess MW, Kuhn V, Degenhart G, Rozman J,Klingenspor M, Hrabe de Angelis M, Valovka T, Huber LA. The negative adipogenesis regulator is transcriptionally regulated by

(TIS7) and translationally by its orthologue (SKMc15).

Elife. 2023 Aug 21;12:e88350. doi: 10.7554/eLife.88350. PMID: 37603466; PMCID: PMC10468205.

The Vietor Laboratory: Regulatory Mechanisms of Cell Differentiation

An Overview of Autophagy in Hematopoietic Stem Cell Transplantation.

Montazersaheb S, Ehsani A, Fathi E, Farahzadi R, Vietor I. Front Bioeng Biotechnol. 2022 May 23;10:849768. doi: 10.3389/fbioe.2022.849768. eCollection 2022. PMID: 35677295.

The negative adipogenesis regulator Dlk1 is transcriptionally regulated by Ifrd1 (TIS7) and translationally by its orthologue Ifrd2 (SKMc15).

Vietor I, Cikes D, Piironen K, Vasakou T, Heimdörfer D, Gstir R, Erlacher MD, Tancevski I, Eller P, Demetz E, Hess MW, Kuhn V, Degenhart G, Rozman J, Klingenspor M, Hrabe de Angelis M, Valovka T, Huber LA.Elife. 2023 Aug 21;12:e88350. doi: 10.7554/eLife.88350.PMID: 37603466.

Granulocyte differentiation of rat bone marrow resident C-kit+ hematopoietic stem cells induced by mesenchymal stem cells could be considered as new option in cell-based therapy.

Farahzadi R, Fathi E, Mesbah-Namin SA, Vietor I. Regen Ther. 2023 May 3;23:94-101. doi: 10.1016/j.reth.2023.04.004. eCollection 2023 Jun. PMID: 37206538.

Adipose Tissue-Mesenchymal Stem Cells Caused to Change the Methylation Status of hTERT Gene Promoter CpG Islands of Molt-4 Leukemia Cells as Cell-based Therapy.

Fathi E, Montazersaheb S, Vandghanooni S, Farahzadi R, Vietor I.Curr Mol Med. 2023;23(3):266-274. doi: 10.2174/1566524022666220118103136.PMID: 35040412

Mesenchymal stem cells cause induction of granulocyte differentiation of rat bone marrow C-kit+ hematopoietic stem cells through JAK3/STAT3, ERK, and PI3K signaling pathways.

Fathi E, Mesbah-Namin SA, Vietor I, Farahzadi R.Iran J Basic Med Sci. 2022 Oct;25(10):1222-1227. doi: 10.22038/IJBMS.2022.66737.14633.PMID: 36311196


L-Carnitine Reduced Cellular Aging of Bone Marrow Resident C-Kit+ Hematopoietic Progenitor Cells Through Telomere Dependent Pathways.

Fathi E, Montazersaheb S, Sanaat Z, Nakhlband A, Vandghanooni S, Farahzadi R, Vietor I.Curr Stem Cell Res Ther. 2023;18(2):231-236. doi: 10.2174/1574888X17666220511141123.PMID: 35546751

Effect of Rat Bone Marrow Derived-Mesenchymal Stem Cells on Granulocyte Differentiation of Mononuclear Cells as Preclinical Agent in Cellbased Therapy.

Fathi E, Azarbad S, Farahzadi R, Javanmardi S, Vietor I.Curr Gene Ther. 2022;22(2):152-161. doi: 10.2174/1566523221666210519111933.PMID: 34011256

 

The Vogel Laboratory: Intracellular Cargo Transport in Congenital Intestinal Diseases

Missense variants in the TRPM7 α-kinase domain are associated with recurrent pediatric acute liver failure.

Schlieben LD, Achleitner MT, Bourke B, Diesner M, Feichtinger RG, Fichtner A, Flechtenmacher C, Hadzic N, Hegarty R, Heilos A, Janecke A, Konstantopoulou V, Lenz D, Mayr JA, Müller T, Prokisch H, Vogel GF. Hepatol Commun. 2024 Nov 29;8(12):e0598. doi: 10.1097/HC9.0000000000000598. eCollection 2024 Dec 1.

Intracellular Trafficking Defects in Congenital Intestinal and Hepatic Diseases.

Szabó L, Pollio AR, Vogel GF. Traffic. 2024 Aug;25(8):e12954. doi: 10.1111/tra.12954.

Kinesin family member 12-related hepatopathy: A generally indolent disorder with elevated gamma-glutamyl-transferase activity.

Vogel GF, Podpeskar A, Rieder D, Salzer H, Garczarczyk-Asim D, Wang L, Abuduxikuer K, Wang JS, Scharrer A, Faqeih EA, Aseeri AT, Vodopiutz J, Heilos A, Pichler J, Huber WD, Müller T, Knisely AS, Janecke AR. Clin Genet. 2024 Sep;106(3):224-233. doi: 10.1111/cge.14524. Epub 2024 Mar 29.

Natural history of Wolcott-Rallison syndrome: A systematic review and follow-up study.

Aldrian D, Bochdansky C, Kavallar AM, Mayerhofer C, Deeb A, Habeb A, Romera Rabasa A, Khadilkar A, Uçar A, Knoppke B, Zafeiriou D, Lang-Muritano M, Miqdady M, Judmaier S, McLin V, Furdela V, Müller T, Vogel GF.

Efficacy of Elimination Diets in Eosinophilic Esophagitis: A Systematic Review and Meta-analysis.

Mayerhofer C, Kavallar AM, Aldrian D, Lindner AK, Müller T, Vogel GF.Clin Gastroenterol Hepatol. 2023 Aug;21(9):2197-2210.e3. doi: 10.1016/j.cgh.2023.01.019. Epub 2023 Jan 31.PMID: 36731591.

A CRISPR screen in intestinal epithelial cells identifies novel factors for polarity and apical transport.

Klee KMC, Hess MW, Lohmüller M, Herzog S, Pfaller K, Müller T, Vogel GF, Huber LA. Elife. 2023 Jan 20;12:e80135. doi: 10.7554/eLife.80135. PMID: 36661306.

The Schmidt Laboratory: Regulation of cellular lipid homeostasis

The structure of the Orm2-containing serine palmitoyltransferase complex reveals distinct inhibitory potentials of yeast Orm proteins. Körner C, Schäfer JH, Esch BM, Parey K, Walter S, Teis D, Januliene D, Schmidt O*, Moeller A*, Fröhlich F*. Cell Rep. 2024 Aug 20;43(8):114627. doi: 10.1016/j.celrep.2024.114627. PMID: 39167489  (* shared corresponding authors)

The Dsc ubiquitin ligase complex identifies transmembrane degrons to degrade orphaned proteins at the Golgi.

Weyer Y, Schwabl SI, Tang X, Purwar A, Siegmann K, Ruepp A, Dunzendorfer-Matt T, Widerin MA, Niedrist V, Mutsters NJM, Tettamanti MG, Weys S, Sarg B, Kremser L, Liedl KR, Schmidt O, Teis D. Nat Commun. 2024 Oct 26;15(1):9257. doi: 10.1038/s41467-024-53676-6. PMID: 39461958

A metabolically controlled contact site between vacuoles and lipid droplets in yeast.
Diep DTV, Collado J, Hugenroth M, Fausten RM, Percifull L, Wälte M, Schuberth C, Schmidt O, Fernández-Busnadiego R, Bohnert M.Dev Cell. 2024 Mar 25;59(6):740-758.e10. doi: 10.1016/j.devcel.2024.01.016. Epub 2024 Feb 16.PMID: 38367622

Targeting the CLK2/SRSF9 splicing axis in prostate cancer leads to decreased ARV7 expression.

Van Goubergen J, Peřina M, Handle F, Morales E, Kremer A, Schmidt O, Kristiansen G, Cronauer MV, Santer FR.Mol Oncol. 2025 Feb;19(2):496-518. doi: 10.1002/1878-0261.13728. Epub 2024 Sep 11.PMID: 39258426

Identification of distinct active pools of yeast serine palmitoyltransferase in sub-compartments of the ER.
Esch BM, Walter S, Schmidt O, Fröhlich F.J Cell Sci. 2023 Dec 1;136(23):jcs261353. doi: 10.1242/jcs.261353. Epub 2023 Dec 19.PMID: 37982431

The Valovka Laboratory: Molecular Basis of Rare Genetic Disorders

The negative adipogenesis regulator Dlk1 is transcriptionally regulated by Ifrd1 (TIS7) and translationally by its orthologue Ifrd2 (SKMc15).

Vietor I, Cikes D, Piironen K, Vasakou T, Heimdörfer D, Gstir R, Erlacher MD, Tancevski I, Eller P, Demetz E, Hess MW, Kuhn V, Degenhart G, Rozman J, Klingenspor M, Hrabe de Angelis M, Valovka T, Huber LA. Elife. 2023 Aug 21;12:e88350. doi: 10.7554/eLife.88350. PMID: 37603466

SLC5A1 Variants in Turkish Patients with Congenital Glucose-Galactose Malabsorption.

Hoşnut FÖ, Janecke AR, Şahin G, Vogel GF, Lafcı NG, Bichler P, Müller T, Huber LA, Valovka T, Aksu AÜ. Genes (Basel). 2023 Jun 27;14(7):1359. doi: 10.3390/genes14071359. PMID: 37510265

Pathogenic Deep Intronic PCSK1 Variant Causes Proprotein Convertase 1/3 Deficiency in a Family.

Huber LM, Subaşıoğlu A, Garczarczyk-Asim D, Valovka T, Müller T, Adam R, Janecke AR.Clin Genet. 2025 Feb 1. doi: 10.1111/cge.14717. Online ahead of print.PMID: 39891480

Anti-inflammatory and cytoprotective polypharmacology of Canephron N reveals targeting of the IKK-NF-κB and p38-MK2-RIPK1 axes.

Milosevic M, Magnutzki A, Braun T, Hussain S, Jakschitz T, Kragl M, Soeberdt M, Nausch B, Bonn GK, Huber LA, Valovka T.Biomed Pharmacother. 2025 Jan;182:117747. doi: 10.1016/j.biopha.2024.117747. Epub 2024 Dec 12.PMID: 39671726

Altered chaperone-nonmuscle myosin II interactions drive pathogenicity of the UNC45A c.710T>C variant in osteo-oto-hepato-enteric syndrome.

Waich S, Kreidl K, Vodopiutz J, Demir AM, Pollio AR, Dostál V, Pfaller K, Parlato M, Cerf-Bensussan N, Adam R, Vogel GF, Uhlig HH, Ruemmele FM, Müller T, Hess MW, Janecke AR, Huber LA, Valovka T. JCI Insight. 2025 Mar 24;10(6):e185508. doi: 10.1172/jci.insight.185508. PMID: 40125554

The Araujo Laboratory: Lysosomal signaling complexes – Coordinating organelle function with cellular homeostasis

Structure of the lysosomal mTORC1-TFEB-Rag-Ragulator megacomplex.

Cui Z, Napolitano G, de Araujo MEG, Esposito A, Monfregola J, Huber LA, Ballabio A, Hurley JH.Nature. 2023 Feb;614(7948):572-579. doi: 10.1038/s41586-022-05652-7. Epub 2023 Jan 25.PMID: 36697823

RagD auto-activating mutations impair MiT/TFE activity in kidney tubulopathy and cardiomyopathy syndrome.

Sambri I, Ferniani M, Campostrini G, Testa M, Meraviglia V, de Araujo MEG, Dokládal L, Vilardo C, Monfregola J, Zampelli N, Vecchio Blanco FD, Torella A, Ruosi C, Fecarotta S, Parenti G, Staiano L, Bellin M, Huber LA, De Virgilio C, Trepiccione F, Nigro V, Ballabio A.Nat Commun. 2023 May 15;14(1):2775. doi: 10.1038/s41467-023-38428-2.PMID: 37188688

Truncated variants of MAGEL2 are involved in the etiologies of the Schaaf-Yang and Prader-Willi syndromes.

Heimdörfer D, Vorleuter A, Eschlböck A, Spathopoulou A, Suarez-Cubero M, Farhan H, Reiterer V, Spanjaard M, Schaaf CP, Huber LA, Kremser L, Sarg B, Edenhofer F, Geley S, de Araujo MEG, Huettenhofer A. Am J Hum Genet. 2024 Jul 11;111(7):1383-1404. doi: 10.1016/j.ajhg.2024.05.023. Epub 2024 Jun 21. PMID: 38908375

The Stasyk Laboratory: Molecular architecture of native lysosomal protein assemblies

DIGE-Based Phosphoproteomic Analysis.

Stasyk T, Huber LA.Methods Mol Biol. 2023;2596:97-104. doi: 10.1007/978-1-0716-2831-7_7.PMID: 36378433

Selection of Funding

The Huber Laboratory: Lysosomal mTOR Signalling – The Crossroads Between Signal Transduction and Endosomal Biogenesis

FWF P 32608 and P 26682, 10.55776/PAT2389124 and FWF DOC 82 doc.fund Cellular Basis of Diseases: Molecular Control of Metabolism and Inflammation
Organelle proteostasis in cellular quiescence and growth SUB4 FWF Grant DOI:10.55776/FG20

New functions of the KICSTOR component SZT2 FWF Grant DOI: 10.55776/PAT2389124

The Vogel Laboratory: Intracellular Cargo Transport in Congenital Intestinal Diseases

ÖNB Anniversary Fund 18019, TWF Grant 0404/2386, ÖGKJ research grant

The Vietor Laboratory: Regulatory Mechanisms of Cell Differentiation

IMPULSE Iran Austria
FWF P36861-B

The Schmidt laboratory: Regulation of cellular lipid homeostasis

Lipotype – Lipid excellence award 2019 (#2)
FWF P36187-B “individual functions of Orm/ORMDL family proteins in membrane homeostasis”

The Stasyk Laboratory: Molecular architecture of native lysosomal protein assemblies

FWF P36975 – Molecular architecture of native LAMTOR and BORC assemblies

The Araujo Laboratory: Lysosomal signalling complexes – Coordinating organelle function with cellular homeostasis

Organelle proteostasis in cellular quiescence and growth SUB5

FWF Grant DOI:10.55776/FG20

TWF GZ F16676/5-2019 – A potential new mechanism for selective modulation of mTORC1

Collaborations

The Huber Laboratory: Lysosomal mTOR Signalling – The Crossroads between Signal Transduction and Endosomal Biogenesis

Giulio Suerti-Furga CeMM, David Haselbach IMP, Manuela Baccarini Max Perutz Laboratories all Vienna Austria
Dagmar Kratky Gottfried Schatz Research Center, Molecular Biology and Biochemistry, Medical University of Graz, AUT

Andrea Ballabio TIGEM, Naples, Italy
Structural Membrane Biology, Jinm Hurley University of California, Berkely, US

The Vogel Laboratory: Intracellular Cargo Transport in Congenital Intestinal Diseases

Saskia Wortmann, Paediatrics, University Hospital Salzburg, AT

The Vietor Laboratory: Regulatory Mechanisms of Cell Differentiation

Ezzatollah Fathi, Department of Clinical Sciences, Faculty of Veterinary Medicine, University of Tabriz, Tabriz, Iran

The Schmidt laboratory: Regulation of cellular lipid homeostasis

Florian Fröhlich, Osnabrück University, DE
Maria Bohnert, Münster University, DE
Robbie Loewith, University of Geneva, CH
Matthias Peter, ETH Zurich, CH

The Valovka Lab: Molecular Basis of Rare Genetic Disorders

Julia Vodopiutz, Department of Pediatrics and Adolescent Medicine, Medical University of Vienna, AUT
Daniel Kotlarz, Department of Pediatrics, Ludwig-Maximilians-Universität (LMU) Munich, DE Christoph Griesbeck, Department of Biotechnology and Food Engineering, MCI – The Entrepreneurial School, AUT
ADSI-Austrian Drug Screening Institute, AUT
Bionorica SE, DE

The Araujo Laboratory: Lysosomal signaling complexes – Coordinating organelle function with cellular homeostasis

Gennaro Napolitano (Tigem, Naples, IT)
David Haselbach (IMP, Vienna, AUT)
Kathrin Thedieck (Institute of Biochemistry,University of Innsbruck, AUT)

The Stasyk Laboratory: Molecular architecture of native lysosomal protein assemblies

Luca Fava (Armenise-Harvard Laboratory of Cell Division, CIBIO Department, University of Trento, IT)