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Vol. 12, Issue 2, 351-365, February 2001
3 QPSXXE Motif
Regulates Signaling, Motility, and Cytoskeletal Engagement
Dana -Farber Cancer Institute and Department of Pathology, Harvard
Medical School, Boston, Massachusetts 02115
Integrin 
3A 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 chains (3A, 6A, 7A), from multiple
species. Phosphorylation of 3A and 6A did not appear to be
directly mediated by protein kinase C (PKC) , 
,
, 
, 
, 
, 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 3-Chinese hamster ovary (CHO) cell adhesion to laminin-5, but did alter 1) 3-dependent tyrosine phosphorylation of focal adhesion kinase and paxillin (in the presence or absence of phorbol 12-myristate 13 acetate stimulation), and p130CAS (in the absence of phorbol
12-myristate 13 acetate stimulation), 2) the shape of cells spread on
laminin-5, and 3) 3-dependent random CHO cell migration on
laminin-5. In addition, S1042A mutation altered the PKC-dependent,
ligand-dependent subcellular distribution of 3 and F-actin in CHO
cells. Together, the results demonstrate clearly that 3A
phosphorylation is functionally relevant. In addition, the results
strongly suggest that 3 phosphorylation may regulate 3
integrin interaction with the cytoskeleton.
Online version of this article contains video
material for Figure 9. Online version is available at
www.molbiolcell.org.
*
Present address: Mario Negri Instituto, Via Eritrea, 62, 20157 Milano, Italy.
Corresponding author. E-mail address:
Martin_Hemler{at}DFCI.Harvard.EDU.
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