Structural and Functional Characterization of Protein I (p362p112) and II (p32) - Calcium/Phospholipid Binding Proteins with Homologies to Lipocortin I

  • Volker Gerke
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 269)


Certain Ca2+-binding proteins, which interact with phospholipids in a Ca2+-dependent manner and are discussed to be involved in the control of membrane fusion events, belong to a newly characterized multigene family (for review see Klee, 1988; Crumpton et al., 1988). Members of this family show a high degree of sequence homology and share a common structural feature : a segment of 70 to 80 amino acids in length, which is repeated either four- or eight-fold (depending on the molecular weight of the individual member). These repeated motifs exhibit homologies with each other, not only within one particular protein, but also between different members of the multigene family. Mild proteolytic cleavage defines two regions in the Ca2+ /lipid-binding proteins : a protease-resistent core, which comprises the repeat motifs, and a short N-terminal tail, which is sensitive to protease and variable in sequence and lenght. While the Ca2+- and phospholipid-binding sites reside in the core, the N-terminal tail often bears tyrosine and/or serine/threonine phosphorylation sites (Glenney and Tack, 1985; De et al., 1986; Gould et al., 1986; Johnsson et al., 1986; Weber et al., 1987). Two major cellular substrates of tyrosine-specific protein kinases belong to this family (for review see Brugge, 1986). p35 is phophorylated by the EGF receptor/kinase. It is identical to lipocortin I, originally described as a steroid-induced inhibitor of phospholipase A2. p36 (also called calpactin I heavy chain, or lipocortin II) is the major cytoplasmic substrate of src-related viral tyrosine kinases. In contrast to other members of this family, p36 forms a tetrametric complex (protein I) with a dimer of a unique pll polypeptide (Erikson et al., 1984; Gerke and Weber, 1984, 1985a). Sequence analysis revealed that p11 belongs to the S-100 family of Ca2+-binding proteins (Gerke and Weber, 1985b; Glenney and Tack, 1985; Hexham et al., 1986). The intact protein I complex (p362p112) was originally isolated from intestinal epithelial cells by exploiting its Ca2+ -dependent interaction with cytoskeletal and/or membrane structures. In addition, a different Ca2+ /lipid-binding protein (protein II) was also found to reside within these cells and was purified following a similar protocol (Gerke and Weber, 1984).


Rous Sarcoma Virus MDBK Cell Membrane Fusion Event Intestinal Brush Border Membrane Vesicle Panel Band 
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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Volker Gerke
    • 1
  1. 1.Max-Planck-Institute for Biophysical ChemistryGoettingenGermany

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