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    Proc Natl Acad Sci U S A. 2001 Sep 11;98(19):10692-7. Epub 2001 Sep 4.

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

    Xu XZ, Moebius F, Gill DL, Montell C.

    Source

    Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

    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 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.

    PMID:
    11535825
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC58528
    Free PMC Article

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