Title

Ponticulin is an atypical membrane protein

UMMS Affiliation

Department of Cell Biology

Date

9-1-1994

Document Type

Article

Subjects

Amino Acid Sequence; Animals; Base Sequence; Carrier Proteins; Cytoplasm; Dictyostelium; Fungal Proteins; Genomic Library; Glycosylphosphatidylinositols; Membrane Glycoproteins; Microfilament Proteins; Molecular Sequence Data; Polymerase Chain Reaction; Protein Structure, Secondary

Disciplines

Cell Biology | Life Sciences | Medicine and Health Sciences

Abstract

We have cloned and sequenced ponticulin, a 17,000-dalton integral membrane glycoprotein that binds F-actin and nucleates actin assembly. A single copy gene encodes a developmentally regulated message that is high during growth and early development, but drops precipitously during cell streaming at approximately 8 h of development. The deduced amino acid sequence predicts a protein with a cleaved NH2-terminal signal sequence and a COOH-terminal glycosyl anchor. These predictions are supported by amino acid sequencing of mature ponticulin and metabolic labeling with glycosyl anchor components. Although no alpha-helical membrane-spanning domains are apparent, several hydrophobic and/or sided beta-strands, each long enough to traverse the membrane, are predicted. Although its location on the primary sequence is unclear, an intracellular domain is indicated by the existence of a discontinuous epitope that is accessible to antibody in plasma membranes and permeabilized cells, but not in intact cells. Such a cytoplasmically oriented domain also is required for the demonstrated role of ponticulin in binding actin to the plasma membrane in vivo and in vitro (Hitt, A. L., J. H. Hartwig, and E. J. Luna. 1994. Ponticulin is the major high affinity link between the plasma membrane and the cortical actin network in Dictyostelium. J. Cell Biol. 126:1433-1444). Thus, ponticulin apparently represents a new category of integral membrane proteins that consists of proteins with both a glycosyl anchor and membrane-spanning peptide domain(s).

Rights and Permissions

Citation: J Cell Biol. 1994 Sep;126(6):1421-31. Link to article on publisher's website

Related Resources

Link to article in PubMed

PubMed ID

8089175

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