Proteomics

Dataset Information

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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 2


Integrins are key plasma membrane proteins that mediate cell-ECM adhesion and communication, and they 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  ...[more]

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