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| Property | Value |
| Name | Calmodulin as a direct detector of Ca2+ signals |
| Description | Many forms of signal transduction occur when Ca2+ enters the cytoplasm of a cell. It has been generally thought that there is a fast buffer that rapidly reduces the free Ca2+ level and that it is this buffered level of Ca2+ that triggers downstream biochemical processes, notably the activation of calmodulin (CaM) and the resulting activation of CaM-dependent enzymes. Given the importance of these transduction processes, it is crucial to understand exactly how Ca2+ activates CaM. We have determined the rate at which Ca2+ binds to CaM and found that Ca2+ binds more rapidly to CaM than to other Ca2+-binding proteins. This property of CaM and its high concentration support a new view of signal transduction: CaM directly intercepts incoming Ca2+ and sets the free Ca2+ level (that is, it strongly contributes to fast Ca2+ buffering) rather than responding to the lower Ca2+ level set by other buffers. This property is crucial for making CaM an efficient transducer. Our results also suggest that other Ca2+ binding proteins have a previously undescribed role in regulating the lifetime of Ca2+ bound to CaM and thereby setting the gain of signal transduction. |
| Filename | Nat Neurosci 2011 FaasCalmodulin as a direct detector of Ca2+ signals.pdf |
| Filesize | 943.77 kB |
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