Proteomics

Dataset Information

0

Proteomic Analysis of Integrin a5 Associated Complexes Dependent upon Integrin Activation State in Zebrafish


ABSTRACT: Integrins are a major class of heterodimeric adhesion receptors composed of an a and b subunit that link the extracellular matrix (ECM) and the cytoskeleton across the cell membrane. When activated by either the intracellular (inside-out signaling) or extracellular (outside-in signaling) environment, integrins undergo a conformational change that increases the ligand binding affinity. As the primary receptor for ECM protein fibronectin, Integrin a5 plays a critical role in zebrafish somitogenesis. To better understand integrin activation in this context, we performed co-immunoprecipitation and Mass Spectrometry (MS) based proteomics using FLAG-tagged Integrin a5 alleles that alter it activation state: constitutive active mutant a5GAAKR and inactive ligand binding deficient mutant a5FYLDD, expressed in maternal zygotic a5 mutant (MZa5-/-) embryos. Our data provide an overview of Integrin associated proteins according to the activation state of the Integrin. This submission contains the raw data files corresponding to PXD024942.

INSTRUMENT(S):

ORGANISM(S): Danio Rerio (zebrafish) (brachydanio Rerio)

TISSUE(S): Embryo

SUBMITTER: Guangyu SUN  

LAB HEAD: Scott A. Holley

PROVIDER: PXD065495 | Pride | 2025-10-13

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
PXD024942.sdrf.tsv Tabular
QEp19-1919_Sun_L31.msf Msf
QEp19-1919_Sun_L31.raw Raw
QEp19-1920_Sun_L32.msf Msf
QEp19-1920_Sun_L32.raw Raw
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Publications

Actn4 links inactive Integrin α5 with actin in zebrafish somites.

Sun Guangyu G   Holley Scott A SA  

Molecular & cellular proteomics : MCP 20251008


Integrins are key plasma membrane proteins mediating cell-ECM adhesion and communication and rely on a conformational change for their activation and bidirectional signaling. However, there are few in vivo studies of integrin activation. Here, we identify Integrin α5 (Itgα5) associated proteins in the physiological setting of zebrafish somite morphogenesis. Using label-free mass spectrometry, we compared Itgα5-associated proteins in different integrin activation states. As expected, we found act  ...[more]

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