Acidic calmodulin binding protein, ACAMP-81, is MARCKS protein interacting with synapsin I

Biochem Biophys Res Commun. 1992 Feb 14;182(3):1395-401. doi: 10.1016/0006-291x(92)91888-w.

Abstract

ACAMP-81 is an acidic calmodulin binding protein with molecular mass of 81 kDa. We report partial amino acid analysis of ACAMP-81 and its interaction with synapsin I. 123 amino acids of ACAMP-81 were determined and the sequence was completely identical with that of MARCKS protein which was thought to be a substrate for calcium/phospholipid dependent protein kinase (PKC). We found ACAMP-81 bound to synapsin I with 125I-labeled ACAMP-81 overlay method. ACAMP-81 bound to the cysteine specific cleaved 51 kDa fragment derived from middle/tail region of synapsin I.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Brain / metabolism*
  • Calmodulin-Binding Proteins / metabolism*
  • Cattle
  • Electrophoresis, Polyacrylamide Gel
  • Intracellular Signaling Peptides and Proteins*
  • Membrane Proteins*
  • Molecular Sequence Data
  • Molecular Weight
  • Myristoylated Alanine-Rich C Kinase Substrate
  • Peptide Fragments / isolation & purification
  • Phosphorylation
  • Proteins / genetics
  • Proteins / isolation & purification
  • Proteins / metabolism*
  • Sequence Homology, Nucleic Acid
  • Synapsins / isolation & purification
  • Synapsins / metabolism*

Substances

  • Calmodulin-Binding Proteins
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Peptide Fragments
  • Proteins
  • Synapsins
  • Myristoylated Alanine-Rich C Kinase Substrate