PMID- 9230930
OWN - NLM
STAT- MEDLINE
DCOM- 19970814
LR  - 20211203
IS  - 1420-682X (Print)
IS  - 1420-682X (Linking)
VI  - 53
IP  - 6
DP  - 1997 Jun
TI  - Participation of annexins in protein phosphorylation.
PG  - 522-6
AB  - Simultaneous discovery of members of the annexin family of calcium and 
      phospholipid binding proteins by several groups is intimately linked to the 
      possibility that these proteins may be controlled by phosphorylation. Indeed, 
      annexin I and annexin II have been identified as major substrates for the 
      tyrosine kinase activity associated with epidermal growth factor receptor (EGF-R) 
      and for the retrovirus encoded protein tyrosine kinase pp60v-arc. Both annexins 
      are also in vitro and/or in situ substrates for platelet derived growth factor 
      (PDGF), insulin and hepatocyte growth factor/scatter factor (HGF/SF) receptor 
      tyrosine kinases. In addition, to serve as substrates for tyrosine protein 
      kinases some annexins are cellular targets for serine threonine protein kinases 
      such as protein kinase C (PKC) and cAMP-dependent protein kinase A (PKA). 
      Although the role of annexin phosphorylation has not been studied in detail, it 
      is thought to influence their vesicle aggregation and phospholipid binding 
      properties. Some annexins are also potent inhibitors of various serine/threonine 
      and tyrosine kinases. The physiological functions of the annexins have still not 
      been clearly defined. Therefore the identification of the ability of these 
      proteins to undergo phosphorylation may be helpful in assigning them a precise 
      biological role.
FAU - Rothhut, B
AU  - Rothhut B
AD  - Equipe de Recherche sur la Biologie Cellulaire et Moleculaire des Mediateurs 
      Lipidiques et des Lipoproteines, C.N.R.S. URA 1283, CHU Saint Antoine, Paris, 
      France. rothhut@ccr.jussieu.fr
LA  - eng
PT  - Journal Article
PT  - Review
PL  - Switzerland
TA  - Cell Mol Life Sci
JT  - Cellular and molecular life sciences : CMLS
JID - 9705402
RN  - 0 (Annexins)
RN  - 0 (Phosphoproteins)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
SB  - IM
MH  - Animals
MH  - Annexins/*physiology
MH  - Humans
MH  - Phosphoproteins/*metabolism
MH  - Phosphorylation
MH  - Protein Serine-Threonine Kinases/*metabolism
MH  - Protein-Tyrosine Kinases/*metabolism
RF  - 51
EDAT- 1997/06/01 00:00
MHDA- 1997/06/01 00:01
CRDT- 1997/06/01 00:00
PHST- 1997/06/01 00:00 [pubmed]
PHST- 1997/06/01 00:01 [medline]
PHST- 1997/06/01 00:00 [entrez]
AID - 10.1007/s000180050066 [doi]
PST - ppublish
SO  - Cell Mol Life Sci. 1997 Jun;53(6):522-6. doi: 10.1007/s000180050066.