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Specific proteolytic cleavage of the myristoylated alanine‐rich C kinase substrate between Asn 147 and Glu 148 also occurs in brain
Author(s) -
Manenti Stéphane,
Taniguchi Hisaaki,
Sorokine Odile,
van Dorsselaer Alain,
Darbon JeanMarie
Publication year - 1997
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/(sici)1097-4547(19970501)48:3<259::aid-jnr8>3.0.co;2-e
Subject(s) - cleavage (geology) , myristoylation , alanine , chemistry , substrate specificity , substrate (aquarium) , biochemistry , phosphorylation , biology , enzyme , amino acid , paleontology , fracture (geology) , ecology
The myristoylated alanine‐rich C kinase substrate (MARCKS) is a major ubiquitous substrate of protein kinase C. The expression of the protein is regulated during cell cycle progression and cell proliferation. Specific proteolytic cleavage of the protein between Asn 147 and Glu 148 was described recently in cultured cells, and the corresponding proteolytic activity was observed in various tissue extracts except for brain. We purified a 40 kDa fragment of MARCKS from bovine brain that we characterized as the C‐terminal specific fragment found in other tissues. The identification of the fragment was achieved by in vitro phosphorylation by protein kinase C, calcium‐dependent interaction with calmodulin, mass spectrometric analysis, and N‐terminal sequencing. These data suggest that specific proteolytic cleavage of MARCKS also occurs in brain and may be a general mechanism of down‐regulation of the protein. J. Neurosci. Res. 48:259–263, 1997. © 1997 Wiley‐Liss, Inc.