Phosphorylation of a Conserved Integrin α3 QPSXXE Motif Regulates Signaling, Motility, and Cytoskeletal EngagementV

Xin A Zhang; Alexa L Bontrager; Christopher S Stipp; Stine-Kathrein Kraeft; Gianfranco Bazzoni; Lan Bo Chen; Martin E Hemler

doi:10.1091/mbc.12.2.351

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Phosphorylation of a Conserved Integrin α3 QPSXXE Motif Regulates Signaling, Motility, and Cytoskeletal EngagementV

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Phosphorylation of a Conserved Integrin α3 QPSXXE Motif Regulates Signaling, Motility, and Cytoskeletal EngagementV

Xin A Zhang, Alexa L Bontrager, Christopher S Stipp, Stine-Kathrein Kraeft, Gianfranco Bazzoni, Lan Bo Chen and Martin E Hemler

Molecular Biology of the Cell, Vol.12(2), pp.351-365

02/2001

DOI: 10.1091/mbc.12.2.351

PMCID: PMC30948

PMID: 11179420

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Abstract

Integrin α3A cytoplasmic tail phosphorylation was mapped to amino acid S1042, as determined by mass spectrometry, and confirmed by mutagenesis. This residue occurs within a “QPSXXE” motif conserved in multiple α chains (α3A, α6A, α7A), from multiple species. Phosphorylation of α3A and α6A did not appear to be directly mediated by protein kinase C (PKC) α, β, γ, δ, ε, ζ, or μ, or by any of several other known serine kinases, although PKC has an indirect role in promoting phosphorylation. A S1042A mutation did not affect α3-Chinese hamster ovary (CHO) cell adhesion to laminin-5, but did alter 1) α3-dependent tyrosine phosphorylation of focal adhesion kinase and paxillin (in the presence or absence of phorbol 12-myristate 13 acetate stimulation), and p130 CAS (in the absence of phorbol 12-myristate 13 acetate stimulation), 2) the shape of cells spread on laminin-5, and 3) α3-dependent random CHO cell migration on laminin-5. In addition, S1042A mutation altered the PKC-dependent, ligand-dependent subcellular distribution of α3 and F-actin in CHO cells. Together, the results demonstrate clearly that α3A phosphorylation is functionally relevant. In addition, the results strongly suggest that α3 phosphorylation may regulate α3 integrin interaction with the cytoskeleton.

Details

Title: Subtitle: Phosphorylation of a Conserved Integrin α3 QPSXXE Motif Regulates Signaling, Motility, and Cytoskeletal EngagementV
Creators: Xin A Zhang - Dana -Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115
Alexa L Bontrager - Dana -Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115
Christopher S Stipp - Dana -Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115
Stine-Kathrein Kraeft - Dana -Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115
Gianfranco Bazzoni - Dana -Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115
Lan Bo Chen - Dana -Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115
Martin E Hemler - Dana -Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115
Resource Type: Journal article
Publication Details: Molecular Biology of the Cell, Vol.12(2), pp.351-365
DOI: 10.1091/mbc.12.2.351
PMID: 11179420
PMCID: PMC30948
NLM abbreviation: Mol Biol Cell
ISSN: 1059-1524
eISSN: 1939-4586
Publisher: The American Society for Cell Biology
Language: English
Date published: 02/2001
Academic Unit: Molecular Physiology and Biophysics; Biology
Record Identifier: 9983992080902771

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