Premium
The major myristoylated PKC substrate (MARCKS) is involved in cell spreading, tyrosine phosphorylation of paxillin, and focal contact formation
Author(s) -
Manenti Stéphane,
Malecaze François,
Darbon Jean-Marie
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01438-5
Subject(s) - marcks , paxillin , focal adhesion , vinculin , phosphorylation , microbiology and biotechnology , tyrosine phosphorylation , myristoylation , tyrosine , protein kinase c , chemistry , biology , biochemistry
The expression of the myristoylated PKC substrate MARCKS is reduced in tumor‐derived choroidal melanoma cells (OCM‐1). We transfected the OCM‐1 cells with MARCKS cDNA and we selected clones with stable overexpression of the protein. Tyrosine phosphorylation of paxillin, a biochemical marker of focal contact formation, was conserved upon serum starvation when MARCKS was overexpressed, while it was almost abolished in the control cells. Immunofluorescent labelling of paxillin and vinculin, another component of focal contact, revealed that these structures were conserved upon serum starvation when MARCKS was overexpressed but not in the control cells. Furthermore, the cell morphology was affected by the ectopic expression of MARCKS, leading to increased spreading and formation of membrane processes. These data suggest the involvement of MARCKS in cell spreading and focal contact formation.