ZF21 Protein Regulates Cell Adhesion and Motility

Cell migration on an extracellular matrix (ECM) requires continuous formation and turnover of focal adhesions (FAs) along the direction of cell movement. However, our knowledge of the components of FAs and the mechanism of their regulation remains limited. Here, we identify ZF21, a member of a prote...

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Bibliographic Details
Published in:The Journal of biological chemistry 2010-07, Vol.285 (27), p.21013-21022
Main Authors: Nagano, Makoto, Hoshino, Daisuke, Sakamoto, Takeharu, Kawasaki, Noritaka, Koshikawa, Naohiko, Seiki, Motoharu
Format: Article
Language:English
Subjects:
Adaptor Proteins, Signal Transducing
Animals
Binding Sites
Carrier Proteins - physiology
Cell Adhesion
Cell Adhesion - physiology
Cell Biology
Cell Line
Cell Membrane - physiology
Cell Migration
Cell Movement - physiology
Cell Surface
Chlorocebus aethiops
COS Cells
Extracellular Matrix
Extracellular Matrix - physiology
Focal Adhesion
Focal Adhesion Kinase 1 - metabolism
Focal Adhesions - physiology
FYVE
Humans
Integrin
Intracellular Signaling Peptides and Proteins - genetics
Membrane Proteins - genetics
Membrane Proteins - physiology
Membrane Type 1 Matrix Metalloproteinase
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Summary:Cell migration on an extracellular matrix (ECM) requires continuous formation and turnover of focal adhesions (FAs) along the direction of cell movement. However, our knowledge of the components of FAs and the mechanism of their regulation remains limited. Here, we identify ZF21, a member of a protein family characterized by the presence of a phosphatidylinositol 3-phosphate-binding FYVE domain, to be a new regulator of FAs and cell movement. Knockdown of ZF21 expression in cells increased the number of FAs and suppressed cell migration. Knockdown of ZF21 expression also led to a significant delay in FA disassembly following induction of synchronous disassembly of FAs by nocodazole treatment. ZF21 bound to focal adhesion kinase, localized to FAs, and was necessary for dephosphorylation of FAK at Tyr397, which is important for disassembly of FAs. Thus, ZF21 represents a new component of FAs, mediates disassembly of FAs, and thereby regulates cell motility.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M110.106443