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

doi:10.1074/jbc.M113.506501

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

Academic Institute

Research output: Contribution to journal › Article › peer-review

58 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 language	English (US)
Pages (from-to)	4262-4272
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	289
Issue number	7
DOIs	https://doi.org/10.1074/jbc.M113.506501
State	Published - Feb 14 2014

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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

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.",

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

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doi = "10.1074/jbc.M113.506501",

language = "English (US)",

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T1 - Drosophila TRPML forms PI(3,5)P2-activated cation channels in both endolysosomes and plasma Membrane

AU - Feng, Xinghua

AU - Huang, Yu

AU - Lu, Yungang

AU - Xiong, Jian

AU - -On Wong, Ching

AU - Yang, Pu

AU - Xia, Jintang

AU - Chen, De

AU - Du, Guangwei

AU - Venkatachalam, Kartik

AU - Xia, Xuefeng

AU - Zhu, Michael X.

PY - 2014/2/14

Y1 - 2014/2/14

N2 - 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.

AB - 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.

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

Abstract

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