In:
FEBS Letters, Wiley, Vol. 381, No. 3 ( 1996-03-04), p. 183-187
Abstract:
To study enzymatic activity and activation conditions of the recently identified novel protein kinase C μ (PKCμ) subtype, epitope tagged PKCμ was propagated in the baculovirus expression system and was purified to homogeneity. PKCμ displays high affinity phorbol ester binding ( K d = 7 nM) resulting in enhanced phosphatidylserine‐dependent kinase activity. From various lipid second messengers known to activate PKCs only diacylglycerol and PtdIns‐4,5‐P 2 , were found to promote PKCμ kinase activity. Two peptides derived from the glycogen synthase, GS‐peptide and syntide 2, were found to be phosphorylated efficiently in vitro. MARCKS (myristoylated alanine‐rich C‐kinase substrate) served as an in vitro substrate for PKCμ too. However, in contrast to other PKCs, a peptide derived from the MARCKS phosphorylation domain is phosphorylated only at serine 156, and not at serines 152 and 163, implicating a differential regulation by PKCμ.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(96)00116-0
Language:
English
Publisher:
Wiley
Publication Date:
1996
detail.hit.zdb_id:
1460391-3
SSG:
12