Lam, A., Galione, A., Lai, Francis Anthony ![]() |
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 |
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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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