Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isoform

X. Z Shawn Xu, Fabian Moebius, Donald L. Gill, Craig Montell

Research output: Contribution to journalArticle

Abstract

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 Ca2+ 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.

Original languageEnglish (US)
Pages (from-to)10692-10697
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume98
Issue number19
DOIs
StatePublished - Sep 11 2001

ASJC Scopus subject areas

  • Genetics
  • General

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