Drosophila TRPML forms PI(3,5)P2-activated cation channels in both endolysosomes and plasma Membrane

Xinghua Feng, Yu Huang, Yungang Lu, Jian Xiong, Ching -On Wong, Pu Yang, Jintang Xia, De Chen, Guangwei Du, Kartik Venkatachalam, Xuefeng Xia, Michael X. Zhu

Research output: Contribution to journalArticlepeer-review

41 Scopus citations

Abstract

Background: Drosophila trpml mutants reproduced many defects associated with mucolipidosis type IV, but the flyTRPML channel remains uncharacterized. Results: Drosophila TRPML is a phosphoinositide-regulated cation channel on endolysosome and plasma membranes. Conclusion: Fly TRPML largely resembles mammalian TRPML1, but exhibits differences in subcellular localization and pH dependence. Significance: The data support using Drosophila for assessing TRPML1 function.

Original languageEnglish (US)
Pages (from-to)4262-4272
Number of pages11
JournalJournal of Biological Chemistry
Volume289
Issue number7
DOIs
StatePublished - Feb 14 2014

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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