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Science 16 April 2004:
Vol. 304. no. 5669, pp. 432 - 435
DOI: 10.1126/science.1093490

Reports

Functional Stoichiometry and Local Enrichment of Calmodulin Interacting with Ca2+ Channels

Masayuki X. Mori, Michael G. Erickson, David T. Yue*

Calmodulin (CaM) interactions with Ca2+ channels mediate both Ca2+ regulation of channels and local Ca2+ triggering of transcription factors implicated in neuronal memory. Crucial to these functions are the number of CaM molecules (CaMs) regulating each channel, and the number of CaMs privy to the local Ca2+ signal from each channel. To resolve these parameters, we fused L-type Ca2+ channels to single CaM molecules. These chimeric molecules revealed that a single CaM directs L-type channel regulation. Similar fusion molecules were used to estimate the local CaM concentration near Ca2+ channels. This estimate indicates marked enrichment of local CaM, as if a "school" of nearby CaMs were poised to enhance the transduction of local Ca2+ entry into diverse signaling pathways.

Ca2+ Signals Laboratory, Departments of Biomedical Engineering and Neuroscience, The Johns Hopkins University School of Medicine, 720 Rutland Avenue, Baltimore, MD 21205, USA.

* To whom correspondence should be addressed. E-mail: dyue{at}bme.jhu.edu

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