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- Publisher Website: 10.1016/j.febslet.2013.10.031
- Scopus: eid_2-s2.0-84887996826
- PMID: 24188827
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Article: Hax-1 identified as a two-pore channel (TPC)-binding protein
Title | Hax-1 identified as a two-pore channel (TPC)-binding protein |
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Authors | |
Keywords | HCLS-associated X-1 Lysosomal ion channel Protein-protein interactions Two-pore channel |
Issue Date | 2013 |
Citation | FEBS Letters, 2013, v. 587, n. 23, p. 3782-3786 How to Cite? |
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. © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
Persistent Identifier | http://hdl.handle.net/10722/343139 |
ISSN | 2023 Impact Factor: 3.0 2023 SCImago Journal Rankings: 1.208 |
DC Field | Value | Language |
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dc.contributor.author | Lam, Andy K.M. | - |
dc.contributor.author | Galione, Antony | - |
dc.contributor.author | Lai, F. Anthony | - |
dc.contributor.author | Zissimopoulos, Spyros | - |
dc.date.accessioned | 2024-05-10T09:05:46Z | - |
dc.date.available | 2024-05-10T09:05:46Z | - |
dc.date.issued | 2013 | - |
dc.identifier.citation | FEBS Letters, 2013, v. 587, n. 23, p. 3782-3786 | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | http://hdl.handle.net/10722/343139 | - |
dc.description.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. © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | - |
dc.language | eng | - |
dc.relation.ispartof | FEBS Letters | - |
dc.subject | HCLS-associated X-1 | - |
dc.subject | Lysosomal ion channel | - |
dc.subject | Protein-protein interactions | - |
dc.subject | Two-pore channel | - |
dc.title | Hax-1 identified as a two-pore channel (TPC)-binding protein | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1016/j.febslet.2013.10.031 | - |
dc.identifier.pmid | 24188827 | - |
dc.identifier.scopus | eid_2-s2.0-84887996826 | - |
dc.identifier.volume | 587 | - |
dc.identifier.issue | 23 | - |
dc.identifier.spage | 3782 | - |
dc.identifier.epage | 3786 | - |
dc.identifier.eissn | 1873-3468 | - |