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Hax‐1 identified as a two‐pore channel (TPC)‐binding protein
Author(s) -
Lam Andy K.M.,
Galione Antony,
Lai F. Anthony,
Zissimopoulos Spyros
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.10.031
Subject(s) - microbiology and biotechnology , mechanism (biology) , intracellular , ion channel , plasma protein binding , transcriptome , biology , biophysics , yeast , chemistry , computational biology , gene , biochemistry , gene expression , receptor , physics , quantum mechanics
Two‐pore channels (TPC1–3) are recently identified endolysosomal ion channels. The mechanism by which these channels are regulated at the molecular level is presently unclear. To identify putative protein regulators of TPCs, we performed unbiased transcriptome‐wide screens using the yeast two‐hybrid technique to identify potential protein–protein interactions with the intracellular domains of human TPC2. We now present biochemical evidence for a novel molecular interaction between human TPC1/2 and the anti‐apoptotic protein Hax‐1 (HCLS‐associated X‐1). The observed binding of Hax‐1 to TPCs may represent a conserved mechanism by which these endolysosomal ion channels are regulated.