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PMID: 17962195 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Gain-of-function mutation in TRPML3 causes the mouse Varitint-Waddler phenotype.

The Journal of biological chemistry ·Vol. 282 ·No. 50 ·2007-12-14 ·Pages 36138-42

Kim HJ, Li Q, Tjon-Kon-Sang S, So I, Kiselyov K, Muallem S

Abstract

TRPML3 is a member of the TRPML subfamily of the transient receptor potential cation channel superfamily. The TRPML3(A419P) mutation causes a severe form, whereas the TRPML3(I362T/A419P) mutation results in a mild form of the varitint-waddler phenotype. The channel properties of TRPML3 and how the mutations cause each phenotype are not known. In this study, we report the first channel properties of TRPML3 as a strongly inward rectifying cation channel with a novel regulation by extracytosolic Na+. Preincubating the extracytosolic face of TRPML3 in Na+-free medium is required for channel activation, but then the channel slowly inactivates. The A419P mutation locks the channel in an open unregulated state. Similar gain of function was observed with the A419G mutation, which, like A419P, is expected to destabilize the alpha-helical fifth transmembrane domain of TRPML3. The I362T mutation results in an inactive channel, but the channel properties of TRPML3(I362T/A419P) are similar to those of TRPML3(A419P). However, the surface expression and current density of TRPML3(I362T/A419P) are lower than those of TRPML3(A419P). The A419P mutation also affects channel glycosylation and causes massive cell death. These findings show that the varitint-waddler phenotype is due to a gain of function of TRPML3(A419P) that is reduced by the TRPML3(I362T/A419P) mutant, resulting in a milder phenotype.

MeSH Terms
Amino Acid Substitution Animals Cell Death/genetics Cell Line Glycosylation Humans Ion Transport/genetics Mice Mucolipidoses/genetics,metabolism Mutation, Missense Phenotype Protein Processing, Post-Translational/genetics Protein Structure, Secondary/genetics Protein Structure, Tertiary/genetics Sodium/metabolism Transient Receptor Potential Channels/genetics,metabolism
Chemicals
MCOLN3 protein, human Transient Receptor Potential Channels Sodium
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Kim Hyun Jin
Department of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
Li Qin
Tjon-Kon-Sang Sandra
So Insuk
Kiselyov Kirill
Muallem Shmuel
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2007-12-14
Epub
2007-00-25
Pages
36138-42
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIDCR NIH HHS · DE12309 · United States
NIDDK NIH HHS · DK38938 · United States
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