ArticleThe Biochemical journal1987
Regulation of calpactin I phospholipid binding by calpactin I light-chain binding and phosphorylation by p60v-src.
Article in The Biochemical journal, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 185 citations in OpenAlex.
- The Annexin A2/S100A10 Complex: The Mutualistic Symbiosis of Two Distinct Proteins.Biomolecules · 2021Review
- The ATP-Releasing Maxi-Cl Channel: Its Identity, Molecular Partners and Physiological/Pathophysiological Implications.Life (Basel, Switzerland) · 2021Review
- Structure of the ALS Mutation Target Annexin A11 Reveals a Stabilising N-Terminal Segment.Biomolecules · 2020Article
- Assessment of the cellular localisation of the annexin A2/S100A10 complex in human placenta.Journal of molecular histology · 2018Article
- Annexin A2 complexes with S100 proteins: structure, function and pharmacological manipulation.British journal of pharmacology · 2015Review
- Lipid segregation and membrane budding induced by the peripheral membrane binding protein annexin A2.The Journal of biological chemistry · 2013Article
- Annexin A2 heterotetramer: structure and function.International journal of molecular sciences · 2013Article
- Annexin A2 at the interface of actin and membrane dynamics: a focus on its roles in endocytosis and cell polarization.International journal of cell biology · 2012Article
- Agents that bind annexin A2 suppress ocular neovascularization.Journal of cellular physiology · 2010Article
- Annexin 2 has a dual role as regulator and effector of v-Src in cell transformation.The Journal of biological chemistry · 2009Article
- Endothelial cell annexin A2 regulates polyubiquitination and degradation of its binding partner S100A10/p11.The Journal of biological chemistry · 2008Article
- The annexin 2/S100A10 complex controls the distribution of transferrin receptor-containing recycling endosomes.Molecular biology of the cell · 2003Article
- Nuclear annexin II negatively regulates growth of LNCaP cells and substitution of ser 11 and 25 to glu prevents nucleo-cytoplasmic shuttling of annexin II.BMC biochemistry · 2003Article
- Annexin II regulates multivesicular endosome biogenesis in the degradation pathway of animal cells.The EMBO journal · 2003Article
- Structural requirements for annexin I-S100C complex-formation.The Biochemical journal · 1996Article
- Annexin II in exocytosis: catecholamine secretion requires the translocation of p36 to the subplasmalemmal region in chromaffin cells.The Journal of cell biology · 1996Article
- Annexin II up-regulates cellular levels of p11 protein by a post-translational mechanisms.The Biochemical journal · 1996Article
- A 42-kilodalton annexin-like protein is associated with plant vacuoles.Plant physiology · 1994Article
- Molecular cloning of a novel N-terminal variant of annexin II from rat basophilic leukaemia cells.The Biochemical journal · 1994Article
- Hyaluronan and the hyaluronan receptor RHAMM promote focal adhesion turnover and transient tyrosine kinase activity.The Journal of cell biology · 1994Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Calpactins I and II are proteins that bind Ca2+, phospholipids, actin and spectrin; they are also major substrates of oncogene and growth-factor-receptor tyrosine kinases. Since calpactins have been proposed to provide a link between membrane lipids and the cytoskeleton, we examined in detail the interactions between purified calpactin I and phospholipid liposomes. We focused on the Ca2+-dependence, the effects of phosphorylation of calpactin I by p60v-src (the protein kinase coded for by the Rous-sarcoma-virus oncogene), and the effects of the binding of calpactin I light chain to calpactin I heavy chain. Binding of the light chain to the heavy chain increased the affinity of calpactin I for phosphatidylserine (PS) liposomes. The opposite effect was observed for phosphorylation by p60v-src; phosphorylation decreased the affinity of calpactin I for PS liposomes. These two opposite effects appeared to be independent, since phosphorylation did not prevent light-chain binding to the heavy chain. Calpactin I was found, by the use of three different techniques, to bind to phospholipid liposomes at less than 10(-8) M free Ca2+. This result is in contrast with those of previous studies, which indicated that greater than 10(-6) M free Ca2+ was required. Our findings suggest that calpactin I may be bound to phospholipids in vivo at Ca2+ concentrations of about 1.5 x 10(-7) M, typical of resting unstimulated cells, and that this interaction may be modulated by light-chain binding and phosphorylation by p60v-src.
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