Protein kinase Cα (PKCα):: Regulation and biological function

被引:219
作者
Nakashima, S [1 ]
机构
[1] Gifu Univ, Sch Med, Dept Biochem, Gifu 5008705, Japan
关键词
apoptosis; differentiation; migration; proliferation; translocation;
D O I
10.1093/oxfordjournals.jbchem.a003272
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein kinase Calpha (PKCalpha) is a serine/threonine kinase and a member of the conventional (classical) PKCs (cPKCs), which have four conserved (C1 to C4) regions. This ubiquitously expressed PKC isotype is activated in response to many different kinds of stimuli and translocates from cytosol to the specialized cellular compartments (nucleus, focal adhesion, caveolae, etc.) where it is presumed to work. Therefore, PKCalpha has been implicated in a variety of cellular functions including proliferation, apoptosis, differentiation, motility, and inflammation. However, the responses induced by activation or overexpression of PKCalpha vary depending on the types, and sometimes conditions, of cells. For example, in some types of cells, PKCalpha is implicated in cell growth. In contrast, it may play a role in cell cycle arrest and differentiation in other types of cells. Therefore, alterations of cell responses induced by PKCalpha are not an intrinsic property of this isoform. The responses are modulated by dynamic interactions with cell-type specific factors: substrates, modulators and anchoring proteins.
引用
收藏
页码:669 / 675
页数:7
相关论文
共 76 条
[1]   Ectopic expression of a mutant form of PKC alpha originally found in human tumors: Aberrant subcellular translocation and effects on growth control [J].
Alvaro, V ;
Prevostel, C ;
Joubert, D ;
Slosberg, E ;
Weinstein, BI .
ONCOGENE, 1997, 14 (06) :677-685
[2]   Involvement of p21Waf1/Cip1 in protein kinase C alpha-induced cell cycle progression [J].
Besson, A ;
Yong, VW .
MOLECULAR AND CELLULAR BIOLOGY, 2000, 20 (13) :4580-4590
[3]   Phosphorylation of protein kinase C-zeta on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state [J].
Bornancin, F ;
Parker, PJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (06) :3544-3549
[4]   2 CLOSELY-RELATED ISOFORMS OF PROTEIN-KINASE-C PRODUCE RECIPROCAL EFFECTS ON THE GROWTH OF RAT FIBROBLASTS - POSSIBLE MOLECULAR MECHANISMS [J].
BORNER, C ;
UEFFING, M ;
JAKEN, S ;
PARKER, PJ ;
WEINSTEIN, IB .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (01) :78-86
[5]   FAILURE OF WILD-TYPE OR A MUTANT FORM OF PROTEIN KINASE-C-ALPHA TO TRANSFORM FIBROBLASTS [J].
BORNER, C ;
FILIPUZZI, I ;
WEINSTEIN, IB ;
IMBER, R .
NATURE, 1991, 353 (6339) :78-80
[6]   Protein phosphatase 2A and protein kinase Cα are physically associated and are involved in Pseudomonas aeruginosa-induced interleukin 6 production by mast cells [J].
Boudreau, RTM ;
Garduno, R ;
Lin, TJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (07) :5322-5329
[7]   PKCα regulates the hypertrophic growth of cardiomyocytes through extracellular signal-regulated kinase1/2 (ERK1/2) [J].
Braz, JC ;
Bueno, OF ;
De Windt, LJ ;
Molkentin, JD .
JOURNAL OF CELL BIOLOGY, 2002, 156 (05) :905-919
[8]  
BUCHNER K, 1995, EUR J BIOCHEM, V228, P211
[9]  
Chang EY, 1997, J IMMUNOL, V159, P2624
[10]   The small GTP-binding protein rho potentiates AP-1 transcription in T cells [J].
Chang, JH ;
Pratt, JC ;
Sawasdikosol, S ;
Kapeller, R ;
Burakoff, SJ .
MOLECULAR AND CELLULAR BIOLOGY, 1998, 18 (09) :4986-4993