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CALM1 — MARCKS

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: MARCKS — CALM1 (association, x-ray crystallography) Yamauchi et al., Nat Struct Biol 2003*
• IRef Hprd Interaction: MARCKS — CALM1 (in vitro) Yamauchi et al., Nat Struct Biol 2003*
• IRef Intact Interaction: Complex of 90 proteins (association, tandem affinity purification) Pichlmair et al., Nature 2012
• IRef Intact Interaction: Complex of 156 proteins (association, anti tag coimmunoprecipitation) Lau et al., Cell 2012

Text-mined interactions from Literome

Matsubara et al., J Biol Chem 2003 : MARCKS , a major in vivo substrate of protein kinase C, interacts with plasma membranes in a phosphorylation-, myristoylation-, and calmodulin dependent manner
Coling et al., Hear Res 1994 : The calmodulin dependent block of MARCKS phosphorylation was observed only in acoustic nerve
Chakravarthy et al., J Biol Chem 1995 (Glioma) : Recently ( Chakravarthy, B. R., Isaacs, R. J., Morley, P., Durkin, J. P., and Whitfield, J. F. ( 1995 ) J. Biol. Chem. 270, 1362-1368 ), we proposed that Ca2+ x calmodulin complexes block MARCKS phosphorylation by the activated PKCs in keratinocytes stimulated by raising the external Ca2+ concentration ... In the present experiments calmodulin prevented MARCKS phosphorylation by TPA stimulated PKCs in glioma cell lysates, and this blockade was lifted by a calmodulin antagonist, the calmodulin binding domain peptide
Yamamoto et al., J Neurochem 1995 : Phosphorylation of MARCKS by protein kinase C inhibited the binding to calmodulin , whereas phosphorylation by cdc2 kinase and TPKII significantly increased the binding to calmodulin
Matsubara et al., FEBS Lett 1998 : MARCKS , a major cellular substrate for protein kinase C, plays important roles in various cellular functions and its functions are regulated by calmodulin