The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Molecular Basis of Calmodulin Tethering and Ca2+-dependent Inactivation of L-type Ca2+ Channels
Open accessAbstract
Ca(2+)-dependent inactivation (CDI) of L-type Ca(2+) channels plays a critical role in controlling Ca(2+) entry and downstream signal transduction in excitable cells. Ca(2+)-insensitive forms of calmodulin (CaM) act as dominant negatives to prevent CDI, suggesting that CaM acts as a resident Ca(2+) sensor. However, it is not known how the Ca(2+) sensor is constitutively tethered. We have found that the tethering of Ca(2+)-insensitive CaM was localized to the C-terminal tail of alpha(1C), close to the CDI effector motif, and that it depended on nanomolar Ca(2+) concentrations, likely attained in quiescent cells. Two stretches of amino acids were found to support the tethering and to contain putative CaM-binding sequences close to or overlapping residues previously shown to affect CDI and Ca(2+)-independent inactivation. Synthetic peptides containing these sequences displayed differences in CaM-binding properties, both in affinity and Ca(2+) dependence, leading us to propose a novel mechanism for CDI. In contrast to a traditional disinhibitory scenario, we suggest that apoCaM is tethered at two sites and signals actively to slow inactivation. When the C-terminal lobe of CaM binds to the nearby CaM effector sequence (IQ motif), the braking effect is relieved, and CDI is accelerated.
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1 retracted
Calmodulin kinase determines calcium-dependent facilitation of L-type calcium channels
Dzhura, I., Wu, Y., Colbran, R. J., Balser, J. R., & Anderson, M. E. (2000) · Nature Cell Biology · doi:10.1038/35004052 · Cited by 335
RetractedTarget Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide Complex
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Calmodulin supports both inactivation and facilitation of L-type calcium channels
Zühlke, R. D., Pitt, G. S., Deisseroth, K., Tsien, R. W., & Reuter, H. (1999) · Nature · doi:10.1038/20200 · Cited by 899
Self-citationSequence motifs for calmodulin recognition
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Mechanism of calcium gating in small-conductance calcium-activated potassium channels
Xia, X.-M., Fakler, B., Rivard, A., Wayman, G., Johnson-Pais, T., Keen, J. E., Ishii, T., Hirschberg, B., Bond, C. T., Lutsenko, S., et al. (1998) · Nature · doi:10.1038/26758 · Cited by 871
Calmodulin Is the Ca2+ Sensor for Ca2+-Dependent Inactivation of L-Type Calcium Channels
Peterson, B. Z., DeMaria, C. D., & Yue, D. T. (1999) · Neuron · doi:10.1016/s0896-6273(00)80709-6 · Cited by 856
Molecular and Structural Basis of Target Recognition by Calmodulin
Crivici, A., & Ikura, M. (1995) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.bb.24.060195.000505 · Cited by 757
Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin
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The Roles of the Subunits in the Function of the Calcium Channel
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Calmodulin bifurcates the local Ca2+ signal that modulates P/Q-type Ca2+ channels
DeMaria, C. D., Soong, T. W., Alseikhan, B. A., Alvania, R. S., & Yue, D. T. (2001) · Nature · doi:10.1038/35078091 · Cited by 407
Cited by
Voltage-Gated Calcium Channels
Catterall, W. A. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003947 · Cited by 1,628
Calcium Cycling and Signaling in Cardiac Myocytes
Bers, D. M. (2008) · Annual Review of Physiology · doi:10.1146/annurev.physiol.70.113006.100455 · Cited by 1,302
Hudmon, A., & Schulman, H. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135410 · Cited by 658
Self-citationCaMKII in myocardial hypertrophy and heart failure
Anderson, M. E., Brown, J. H., & Bers, D. M. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.01.012 · Cited by 465
Erickson, M. G., Alseikhan, B. A., Peterson, B. Z., & Yue, D. T. (2001) · Neuron · doi:10.1016/s0896-6273(01)00438-x · Cited by 465
Metadata
- Authors
- Pitt, G. S., Zühlke, R. D., Hudmon, A., Schulman, H., Reuter, H., & Tsien, R. W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-08
- Volume
- 276
- Issue
- 33
- Pages
- 30794-30802
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2086871275
- Cited by
- 294
- References
- 31
- FWCI
- 7.38
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Pitt, G. S., Zühlke, R. D., Hudmon, A., Schulman, H., Reuter, H., & Tsien, R. W. (2001). Molecular Basis of Calmodulin Tethering and Ca2+-dependent Inactivation of L-type Ca2+ Channels. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m104959200
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