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A novel c-Src recruitment pathway from the cytosol to focal adhesions.
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- Additional Information
- Source:
Publisher: John Wiley & Sons Ltd Country of Publication: England NLM ID: 0155157 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-3468 (Electronic) Linking ISSN: 00145793 NLM ISO Abbreviation: FEBS Lett Subsets: MEDLINE
- Publication Information:
Publication: Jan. 2016- : West Sussex : John Wiley & Sons Ltd.
Original Publication: Amsterdam, North-Holland on behalf of the Federation of European Biochemical Societies.
- Subject Terms:
- Abstract:
The role of myristoylation in the localization and catalytic activity of Src at focal adhesions was investigated by live-cell imaging and site-directed mutagenesis. Although the majority of activated Src molecules are localized at focal adhesions, it is unclear how activated Src molecules are recruited to focal adhesions. Because Src is activated at the cell membrane, translocation of Src to cell membranes is considered to be essential for its recruitment to focal adhesions. Membrane-targeting-deficient Src mutant SrcG2A localizes at focal adhesions, indicating direct recruitment of Src from cytosol to focal adhesions. Furthermore, directly recruited Src molecules are shown to enhance paxillin dynamics at focal adhesions. These results reveal that the regulation of Src activation and translocation is more complex than previously suggested.
(© 2017 Federation of European Biochemical Societies.)
- Contributed Indexing:
Keywords: TIRF; FRAP; focal adhesion; mechanobiology; mechanotransduction
- Accession Number:
0I3V7S25AW (Myristic Acid)
EC 2.7.10.2 (CSK Tyrosine-Protein Kinase)
EC 2.7.10.2 (Focal Adhesion Kinase 1)
EC 2.7.10.2 (PTK2 protein, human)
EC 2.7.10.2 (src-Family Kinases)
EC 2.7.10.23 (CSK protein, human)
- Publication Date:
Date Created: 20170526 Date Completed: 20170818 Latest Revision: 20191210
- Publication Date:
20221213
- Accession Number:
10.1002/1873-3468.12696
- Accession Number:
28543306
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