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Analysis of podocyte adhesome proteomes

ABSTRACT: To elucidate potential mechanisms how EPB41L5 modulates integrin adhesion complex maturation, we performed quantitative SILAC-based integrin adhesome proteomics. For MS analysis of the podocyte adhesome, EPB41L5 or Luciferase (as negative control) was transient expressed in SILAC labeled podocytes by nucleofection (Amaxa Nucleofector, Lonza, Switzerland). Podocytes were seeded on cell culture dishes for 24 hours. Isolation of integrin adhesion complexes from podocytes was performed prior LC-MSMS analysis.In a second set of experiments adhesion complexes of collagen IV and fibronectin coated dishes were purified and analysed by LC-MSMS.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Podocyte (sensu Diptera)

SUBMITTER: Joern Dengjel

LAB HEAD: Joern Dengjel

PROVIDER: PXD023821 | Pride | 2021-08-05

REPOSITORIES: Pride

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			Action	DRS
	20140416_VKNT2_A_01.RAW	Raw
	20140416_VKNT2_A_02.RAW	Raw
	20140416_VKNT2_A_03.RAW	Raw
	20140416_VKNT2_A_04.RAW	Raw
	20140416_VKNT2_A_05.RAW	Raw

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Publications

EPB41L5 controls podocyte extracellular matrix assembly by adhesome-dependent force transmission.

Maier Jasmin I JI Rogg Manuel M Helmstädter Martin M Sammarco Alena A Schilling Oliver O Sabass Benedikt B Miner Jeffrey H JH Dengjel Jörn J Walz Gerd G Werner Martin M Huber Tobias B TB Schell Christoph C

Cell reports 20210301 12

The integrity of the kidney filtration barrier essentially relies on the balanced interplay of podocytes and the glomerular basement membrane (GBM). Here, we show by analysis of in vitro and in vivo models that a loss of the podocyte-specific FERM-domain protein EPB41L5 results in impaired extracellular matrix (ECM) assembly. By using quantitative proteomics analysis of the secretome and matrisome, we demonstrate a shift in ECM composition characterized by diminished deposition of core GBM compo ...[more]

PMID: 33761352

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EPB41L5 controls podocyte extracellular matrix assembly by promoting integrin adhesome reinforcement - CCM dataset

Project description:The integrity of the kidney filtration barrier essentially relies on the balanced interplay of podocytes, endothelial cells and the glomerular basement membrane. Dysfunction in any of these components results in proteinuria and can progress to chronic kidney disease. While the relevance of cell-matrix interactions for podocytes is well established, it is only incompletely understood whether and how adhesion receptors reciprocally influence the basement membrane and maintain glomerular function. Here, we show by analysis of in vitro and in vivo models that a loss of the podocyte specific FERM-domain protein EPB41L5 results in impaired extracellular matrix integrity and stability. Employing quantitative proteomics analysis of the secretome, matrisome and integrin adhesome revealed that EPB41L5 promotes mechanosensitive properties of podocyte integrin complexes by recruitment of PDLIM5/ACTN4. Consecutively, EPB41L5 knockout podocytes showed insufficient reinforcement of integrin adhesion sites, which translated into impaired ECM assembly. These observations build the framework for a model where EPB41L5 as a cell type specific regulator of the podocyte adhesome controls a localized adaptive module in order to prevent podocyte detachment and ensures GBM integrity.

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The melanoma cell line MDA-MB-435 adhesome in long-term culture and its comparison to the adhesome upon integrin αV knockdown

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Characterisation of a nucleo-adhesome

Project description:In addition to central functions in cell adhesion signalling, integrin-associated proteins have wider roles at sites distal to adhesion receptors. In experimentally defined adhesomes, we noticed that there is clear enrichment of proteins that localise to the nucleus, and conversely, we now report that nuclear proteomes contain a class of adhesome components that localise to the nucleus. We here defined a nucleo-adhesome, providing experimental evidence for a remarkable scale of nuclear localisation of adhesion proteins, establishing a framework for interrogating nuclear adhesion protein functions.

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