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Sequence motifs for calmodulin recognition
Abstract
Calmodulin (CaM) is recognized as a major calcium sensor and orchestrator of regulatory events through its interaction with a diverse group of cellular proteins. Many investigations have focused on defining the region of interaction between CaM and its cellular targets and the action of CaM on target protein function. Because CaM can bind with high affinity to a relatively small α‐helical region of many proteins, success in clearly defining the essential elements of CaM binding motifs seems feasible and should provide a means of identifying CaM binding proteins. Three recognition motifs for CaM interaction are discussed in the context of experimental investigations of a variety of CaM target proteins. A modified version of the IQ motif as a consensus for Ca 2+ ‐independent binding and two related motifs for Ca 2+ ‐dependent binding, termed 18‐14 and 1‐5‐10 based on the position of conserved hydrophobic residues, are proposed. Although considerable sequence diversity is observed among the different binding regions, these three classes of recognition motifs exist for many of the known CaM binding proteins.—Rhoads, A. R., Friedberg, F. Sequence motifs for calmodulin recognition. FASEB J. 11, 331‐340 (1997)
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Cites
Calmodulin Trapping by Calcium-Calmodulin-Dependent Protein Kinase
Meyer, T., Hanson, P. I., Stryer, L., & Schulman, H. (1992) · Science · doi:10.1126/science.256.5060.1199 · Cited by 637
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Metadata
- Authors
- Rhoads, A. R., & Friedberg, F.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 1997-04
- Volume
- 11
- Issue
- 5
- Pages
- 331-340
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W2120385383
- Cited by
- 880
- References
- 1
- FWCI
- 11.36
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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