%0 Journal Article %1 Mori_2004_432 %A Mori, Masayuki X %A Erickson, Michael G %A Yue, David T %D 2004 %J Science %K AMP Calcium Calcium; Calmodulin; Cell Channels, Cyclic Element-Binding Energy Fluorescence Fusion Humans; L-Type; Line; Mathematics; Mutation; Nucleus; Patch-Clamp Peptides; Protein Protein; Proteins; Recombinant; Resonance Response Signaling; Structure, Techniques; Tertiary; Transfection Transfer; %N 5669 %P 432--435 %R 10.1126/science.1093490 %T Functional stoichiometry and local enrichment of calmodulin interacting with Ca$^2+$ channels. %U http://dx.doi.org/10.1126/science.1093490 %V 304 %X Calmodulin (CaM) interactions with Ca$^2+$ channels mediate both Ca$^2+$ regulation of channels and local Ca$^2+$ 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 Ca$^2+$ signal from each channel. To resolve these parameters, we fused L-type Ca$^2+$ 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 Ca$^2+$ channels. This estimate indicates marked enrichment of local CaM, as if a "school" of nearby CaMs were poised to enhance the transduction of local Ca$^2+$ entry into diverse signaling pathways.

@article{Mori_2004_432, abstract = {Calmodulin (CaM) interactions with {C}a$^{2+}$ channels mediate both {C}a$^{2+}$ regulation of channels and local {C}a$^{2+}$ 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 {C}a$^{2+}$ signal from each channel. To resolve these parameters, we fused L-type {C}a$^{2+}$ 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 {C}a$^{2+}$ channels. This estimate indicates marked enrichment of local CaM, as if a "school" of nearby CaMs were poised to enhance the transduction of local {C}a$^{2+}$ entry into diverse signaling pathways.}, added-at = {2009-06-03T11:20:58.000+0200}, author = {Mori, Masayuki X and Erickson, Michael G and Yue, David T}, biburl = {https://www.bibsonomy.org/bibtex/233645d2e95c120b033b0bcb0cdcfbbc5/hake}, description = {The whole bibliography file I use.}, doi = {10.1126/science.1093490}, file = {Mori_2004_432.pdf:Mori_2004_432.pdf:PDF;Mori_2004_432.pdf:Mori_2004_432.pdf:PDF}, institution = {{C}a$^{2+}$ Signals Laboratory, Department of Biomedical Engineering , Johns Hopkins University School of Medicine, 720 Rutland Avenue, Baltimore, MD 21205, USA.}, interhash = {a0ce5be1b2c9ee486173b63ed041599d}, intrahash = {33645d2e95c120b033b0bcb0cdcfbbc5}, journal = {Science}, keywords = {AMP Calcium Calcium; Calmodulin; Cell Channels, Cyclic Element-Binding Energy Fluorescence Fusion Humans; L-Type; Line; Mathematics; Mutation; Nucleus; Patch-Clamp Peptides; Protein Protein; Proteins; Recombinant; Resonance Response Signaling; Structure, Techniques; Tertiary; Transfection Transfer;}, month = Apr, number = 5669, pages = {432--435}, pii = {304/5669/432}, pmid = {15087548}, timestamp = {2009-06-03T11:21:23.000+0200}, title = {Functional stoichiometry and local enrichment of calmodulin interacting with {C}a$^{2+}$ channels.}, url = {http://dx.doi.org/10.1126/science.1093490}, volume = 304, year = 2004 }