Proteomics

Dataset Information

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Integrin a5, aV, and aVb3 in zebrafish embryos at the 12 somite stage


ABSTRACT: Integrins are a major class of heterodimeric adhesion receptors composed of an a and b subunit that mediate cell adhesion to the extracellular matrix (ECM). The extracellular matrix protein fibronectin is important for early vertebrate development, and Integrin a5b1 and aVb3 are the two primary fibronectin receptors. To better define the integrin – ECM protein network at 10-13 somite stage of zebrafish development, we performed co-immunoprecipitation and Mass Spectrometry (MS) based proteomics using FLAG-tagged Integrin a5, aV, and aVb3 expressed in maternal zygotic a5 mutant (MZa5-/-) embryos. We found that Integrin a5b1 and aVb1 are the functional fibronectin receptors, whereas Integrin aVb3 displayed low affinity to both fibronectins (Fn1a and Fn1b). In addition, basement membrane ligands Laminins (lama1, lamb1a, lamc1) are roughly equal in all three datasets while Thrombospondins (thbs3b, thbs4b) and cartilage oligomeric matrix protein (comp/thbs5) are found exclusively in the aV dataset. Our results suggest a diverse role of aV class integrins in ECM protein recruitment.

INSTRUMENT(S): Q Exactive

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

SUBMITTER: Scott Holley  

LAB HEAD: Scott A. Holley

PROVIDER: PXD024665 | Pride | 2021-09-10

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
QEp18-5924_Sun_I22-_1_.msf Msf
QEp18-5924_Sun_I22-_1_.mzid Mzid
QEp18-5924_Sun_I22-_1_.mzid_QEp18-5924_Sun_I22-_1_.MGF Mzid
QEp18-5925_Sun_I21-_1_.msf Msf
QEp18-5925_Sun_I21-_1_.mzid Mzid
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Publications

Integrin intra-heterodimer affinity inversely correlates with integrin activatability.

Sun Guangyu G   Guillon Emilie E   Holley Scott A SA  

Cell reports 20210601 10


Integrins are heterodimeric cell surface receptors composed of an α and β subunit that mediate cell adhesion to extracellular matrix proteins such as fibronectin. We previously studied integrin α5β1 activation during zebrafish somitogenesis, and in the present study, we characterize the integrin αV fibronectin receptors. Integrins are activated via a conformational change, and we perform single-molecule biophysical measurements of both integrin activation via fluorescence resonance energy transf  ...[more]

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