Mapping the domain structure of human erythrocyte adducin.

Journal Article (Journal Article)

Adducin is a 200-kDa heterodimeric protein associated with the erythrocyte membrane skeleton which binds to Ca2+/calmodulin, promotes binding of spectrin to actin, and is a substrate for protein kinases C and A. Adducin polypeptides can be structurally and functionally divided into two distinct regions. The amino-terminal 39-kDa domain of each subunit is more basic and resistant to proteases than the C-terminal 60-64-kDa domain, which is very sensitive to proteolytic degradation. Two-dimensional peptide map analysis revealed that the 39-kDa protease-resistant domains represent a portion of adducin which is highly conserved between the alpha and beta subunits whereas the protease-sensitive regions are different in each subunit. Comparison of the structural and functional properties of purified 39-kDa domains with intact adducin showed that the 39-kDa domains were not phosphorylated by protein kinases C or A and did not bind to Ca2+/calmodulin or interact with spectrin and actin. This suggests that the protease-sensitive domains may perform the various functions of adducin since these activities were all lacking from the protease-resistant domains. It is also possible that the conserved and variable domains are both required for one or more activities of adducin or that the 39-kDa domains play a role in maintaining the oligomeric state of adducin necessary for interaction of the variable domains with spectrin-actin complexes.

Full Text

Duke Authors

Cited Authors

  • Joshi, R; Bennett, V

Published Date

  • August 5, 1990

Published In

Volume / Issue

  • 265 / 22

Start / End Page

  • 13130 - 13136

PubMed ID

  • 2376589

International Standard Serial Number (ISSN)

  • 0021-9258


  • eng

Conference Location

  • United States