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Hax-1 identified as a two-pore channel (TPC)-binding protein

Lam, A., Galione, A., Lai, Francis Anthony ORCID: https://orcid.org/0000-0003-2852-8547 and Zissimopoulos, Spyros 2013. Hax-1 identified as a two-pore channel (TPC)-binding protein. FEBS Letters 587 (23) , pp. 3782-3786. 10.1016/j.febslet.2013.10.031

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Abstract

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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Subjects: R Medicine > R Medicine (General)
R Medicine > RZ Other systems of medicine
Uncontrolled Keywords: Adaptor Proteins Signal Transducing;Calcium Channels;Gene Deletion;HEK293 Cells;Humans;ProteinBinding;Protein StructureTertiary
Additional Information: EMTREE drug terms: binding protein; Hax 1 protein; ion channel; TPC1 protein; TPC2 protein; transcriptome; two pore channel binding protein; unclassified drug EMTREE medical terms: article; controlled study; human; human cell; nonhuman; priority journal; protein binding; protein domain; protein protein interaction Medline keywords: activation domain; AD; glutathione S-transferase; GST; HCLS-associated X-1; inositol trisphosphate; IP(3); Lysosomal ion channel; NAADP; nicotinic acid adenine dinucleotide phosphate; phosphoinositide-3,5-bisphosphate; PI(3,5)P(2); Protein-protein interactions; sarcoplasmic reticulum Ca(2+)-ATPase; SERCA; TM; transmembrane; Two-pore channel Medline is the source for the MeSH terms of this document.
Publisher: Elsevier
ISSN: 0014-5793
Last Modified: 28 Oct 2022 09:27
URI: https://orca.cardiff.ac.uk/id/eprint/74602

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