A GROWTH-DEPENDENT POSTTRANSLATIONAL MODIFICATION OF ANNEXIN-VI

被引:17
作者
MOSS, SE [1 ]
JACOB, SM [1 ]
DAVIES, AA [1 ]
CRUMPTON, MJ [1 ]
机构
[1] IMPERIAL CANC RES FUND, LONDON WC2A 3PX, ENGLAND
关键词
ANNEXIN; LIPOCORTIN; CALPACTIN; POSTTRANSLATIONAL MODIFICATION;
D O I
10.1016/0167-4838(92)90045-F
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
Annexin VI (p68, 67-kDa calelectrin) is a member of a family of Ca2+/phospholipid-binding proteins, that includes p35 (annexin I) and p36 (annexin II), the major cellular substrates for phosphorylation by the epidermal growth factor receptor and pp60v-src tyrosine kinase activities, respectively. We report here that like annexins I and II, annexin VI is phosphorylated in vivo, but that in contrast, annexin VI phosphorylation is associated with cell growth. In both Swiss 3T3 fibroblasts and human T-lymphoblasts the pattern of phosphorylation followed an almost identical profile. In particular, annexin VI was not phosphorylated in quiescent cells, but was phosphorylated on serine and to a lesser extent threonine, several hours following cell stimulation. Furthermore, annexin VI also incorporated phosphate in a growth-dependent manner, in a form other than a phosphoamino-acid. The phosphate was visualised following acid hydrolysis of immunoprecipitated annexin VI, as part of a complex having high mobility on 2-D thin-layer electrophoresis. The identity of this complex is not known. The results suggest that a post-translational modification other than direct protein phosphorylation may influence the activity of annexin VI and provide evidence linking cell growth with regulation of annexin VI function.
引用
收藏
页码:120 / 126
页数:7
相关论文
共 30 条
[1]   IDENTIFICATION OF CALCIUM-DEPENDENT PHOSPHOLIPID-BINDING PROTEINS IN HIGHER-PLANT CELLS [J].
BOUSTEAD, CM ;
SMALLWOOD, M ;
SMALL, H ;
BOWLES, DJ ;
WALKER, JH .
FEBS LETTERS, 1989, 244 (02) :456-460
[2]   TOO SOON FOR CONSENSUS [J].
BROWNING, J ;
PEPINSKY, B ;
WALLNER, B ;
FLOWER, RJ ;
PEERS, SH .
NATURE, 1990, 346 (6282) :324-324
[3]   THE RETINOBLASTOMA PROTEIN IS PHOSPHORYLATED DURING SPECIFIC PHASES OF THE CELL-CYCLE [J].
BUCHKOVICH, K ;
DUFFY, LA ;
HARLOW, E .
CELL, 1989, 58 (06) :1097-1105
[4]   THE INTERLEUKIN-2 T-CELL SYSTEM - A NEW CELL-GROWTH MODEL [J].
CANTRELL, DA ;
SMITH, KA .
SCIENCE, 1984, 224 (4655) :1312-1316
[5]   DIVERSITY IN THE LIPOCORTIN CALPACTIN FAMILY [J].
CROMPTON, MR ;
MOSS, SE ;
CRUMPTON, MJ .
CELL, 1988, 55 (01) :1-3
[6]   PRIMARY STRUCTURE OF THE HUMAN, MEMBRANE-ASSOCIATED CA-2+-BINDING PROTEIN-P68 - A NOVEL MEMBER OF A PROTEIN FAMILY [J].
CROMPTON, MR ;
OWENS, RJ ;
TOTTY, NF ;
MOSS, SE ;
WATERFIELD, MD ;
CRUMPTON, MJ .
EMBO JOURNAL, 1988, 7 (01) :21-27
[7]  
CRUMPTOM MJ, 1990, NATURE, V45, P212
[8]  
DAVIDSON FF, 1987, J BIOL CHEM, V262, P1698
[9]   BIOLOGICAL RELEVANCE OF LIPOCORTINS AND RELATED PROTEINS AS INHIBITORS OF PHOSPHOLIPASE-A2 [J].
DAVIDSON, FF ;
DENNIS, EA .
BIOCHEMICAL PHARMACOLOGY, 1989, 38 (21) :3645-3651
[10]   NONIDET P-40 EXTRACTION OF LYMPHOCYTE PLASMA-MEMBRANE - CHARACTERIZATION OF THE INSOLUBLE RESIDUE [J].
DAVIES, AA ;
WIGGLESWORTH, NM ;
ALLAN, D ;
OWENS, RJ ;
CRUMPTON, MJ .
BIOCHEMICAL JOURNAL, 1984, 219 (01) :301-308