|
| Publications [#112859] of G Vann V. Bennett
Papers Published
- R Joshi, V Bennett, Mapping the domain structure of human erythrocyte adducin.,
The Journal of biological chemistry, UNITED STATES, vol. 265 no. 22
(August, 1990),
pp. 13130-6, ISSN 0021-9258
(last updated on 2003/02/18)
Abstract:
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.
Keywords:
Blood Proteins • Calmodulin-Binding Proteins • Chymotrypsin • Electrophoresis, Gel, Two-Dimensional • Electrophoresis, Polyacrylamide Gel • Erythrocytes • Humans • Macromolecular Substances • Molecular Weight • Peptide Fragments • Peptide Mapping • Protein Conformation • Trypsin • genetics* • isolation & purification • metabolism*
|
