A genetic modifier links integrin a5 to the phenotypic variability of fibronectin 1a mutant zebrafish
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ABSTRACT:
PROVIDER: PRJEB89164 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| ERR14938987_1.fastq.gz | Fastqsanger.gz | |||
| ERR14938987_2.fastq.gz | Fastqsanger.gz | |||
| ERR14938988_1.fastq.gz | Fastqsanger.gz | |||
| ERR14938988_2.fastq.gz | Fastqsanger.gz |
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Project description: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.
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Project description: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.
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