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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
2001-9-12
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pubmed:databankReference |
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pubmed:abstractText |
The TRP (transient receptor potential) superfamily includes a group of subfamilies of channel-like proteins mediating a multitude of physiological signaling processes. The TRP-melastatin (TRPM) subfamily includes the putative tumor suppressor melastatin (MLSN) and is a poorly characterized group of TRP-related proteins. Here, we describe the identification and characterization of an additional TRPM protein TRPM4. We reveal that TRPM4 and MLSN each mediate Ca(2+) entry when expressed in HEK293 cells. Furthermore, we demonstrate that a short form of MLSN (MLSN-S) interacts directly with and suppresses the activity of full-length MLSN (MLSN-L). This suppression seems to result from the inhibition of translocation of MLSN-L to the plasma membrane. We propose that control of translocation through interaction between MLSN-S and MLSN-L represents a mode for regulating ion channel activity.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-10488066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-10607831,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-10611962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-10717675,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-10744543,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-10764638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-10821274,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-10896160,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-10903843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-11025659,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-11081638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-11094154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-11112208,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-11112417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-11161216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-11175743,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-11208852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-11385574,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-11385575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-1314617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-2516726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-9215637,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-9334401,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-9537257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-9806836,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11535825-9806837
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
98
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10692-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11535825-Amino Acid Sequence,
pubmed-meshheading:11535825-Calcium,
pubmed-meshheading:11535825-Calcium Channels,
pubmed-meshheading:11535825-Cation Transport Proteins,
pubmed-meshheading:11535825-Cell Line,
pubmed-meshheading:11535825-Cytoplasm,
pubmed-meshheading:11535825-Humans,
pubmed-meshheading:11535825-Membrane Proteins,
pubmed-meshheading:11535825-Molecular Sequence Data,
pubmed-meshheading:11535825-Neoplasm Proteins,
pubmed-meshheading:11535825-Protein Isoforms,
pubmed-meshheading:11535825-TRPM Cation Channels
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pubmed:year |
2001
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pubmed:articleTitle |
Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isoform.
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pubmed:affiliation |
Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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