Interaction of smooth muscle caldesmon with phospholipids.
Taking into account the perimembrane localization of caldesmon [(1986) Nature 319, 68] and its ability to participate in the regulation of receptor clusterization [(1989) J. Biol. Chem. 264, 496], we studied the interaction of duck gizzard caldesmon with soybean phospholipids (azolectin). By using four independent methods, i.e. light scattering, gel-electrophoresis, gel-filtration and ultracentrifugation, we showed a Ca-independent complex formation between caldesmon and azolectin. Interacting with caldesmon, calmodulin is shown to dissociate the caldesmon-azolectin complex. It is supposed that the caldesmon-phospholipid interaction may affect caldesmon phosphorylation by Ca-phospholipid-dependent protein kinase. This effect may be important for various cell motility processes.
Vorotnikov
A V
AV
Department of Biochemistry, School of Biology, Moscow State University, USSR.
Gusev
N B
NB
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002148:Calmodulin-Binding Proteins / Q000378:metabolism*; D002850:Chromatography, Gel; D004586:Electrophoresis; D000070559:Gizzard, Non-avian; D066298:In Vitro Techniques; D008027:Light; D009130:Muscle, Smooth; D010713:Phosphatidylcholines; D010743:Phospholipids / Q000378:metabolism*; D012542:Scattering, Radiation; D014461:Ultracentrifugation
D002148:Calmodulin-Binding Proteins; D010713:Phosphatidylcholines; D010743:Phospholipids; C024990:asolectin; D002118:Calcium