Results 11 to 20 of about 709 (136)

TRPML3/BK complex promotes autophagy and bacterial clearance by providing a positive feedback regulation of mTOR via PI3P [PDF]

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2023
TRPML3 is a Ca 2+ /Na + release channel residing in both phagophores and endolysosomal membranes. It is activated by PI3P and PI3,5P2.
Christian Grimm   +2 more
exaly   +5 more sources

MCOLN3/TRPML3 bridges the regulation of autophagosome biogenesis by PtdIns3P and the calcium channel [PDF]

open access: yesAutophagy, 2023
In recent years, an increasing number of studies have started to investigate the roles of ions and ion channels in macroautophagy/autophagy. One finding is that calcium regulates multiple stages of autophagy with lysosomal calcium release being important for autophagosome and lysosome fusion.
Daniel Klionsky
exaly   +4 more sources

TRPML3 and hearing loss in the varitint-waddler mouse [PDF]

open access: yesBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 2007
TRPML3 (also known as mucolipin-3, MCOLN3) belongs to the small family of TRPML ion channel proteins. The mammalian Trpml3 gene encodes a protein of 553 amino acids with short amino and carboxy termini and a transient receptor potential motif spanning from the third to the sixth trans membrane domain.
Atiba-Davies, Margaret   +1 more
openaire   +4 more sources

Whole-body analysis of TRPML3 (MCOLN3) expression using a GFP-reporter mouse model reveals widespread expression in secretory cells and endocrine glands [PDF]

open access: yesPLoS ONE, 2022
TRPML3 (mucolipin 3, MCOLN3) is an endolysosomal cation channel belonging to the TRPML subfamily of transient receptor potential channels. Gain-of-function mutations in the Trpml3 gene cause deafness, circling behavior and coat color dilution in mice due to cell death of TRPML3-expressing hair cells of the inner ear or skin melanocytes, respectively ...
Christian Grimm   +2 more
exaly   +4 more sources

Palmitoylation controls trafficking of the intracellular Ca2+ channel MCOLN3/TRPML3 to regulate autophagy [PDF]

open access: yesAutophagy, 2018
MCOLN3/TRPML3 is a Ca2+-permeable cation channel that is expressed in multiple subcellular compartments with dynamic localization. Our previous studies suggest that upon macroautophagy/autophagy induction MCOLN3/TRPML3 is recruited and provides Ca2+ for the fusion process in autophagosome biogenesis.
So Woon Kim   +7 more
openaire   +3 more sources

A helix-breaking mutation in TRPML3 leads to constitutive activity underlying deafness in the varitint-waddler mouse [PDF]

open access: yesProceedings of the National Academy of Sciences, 2007
Homozygote varitint-waddler ( Va ) mice, expressing a mutant isoform (A419P) of TRPML3 (mucolipin 3), are profoundly deaf and display vestibular and pigmentation deficiencies, sterility, and perinatal lethality.
Christian, Grimm   +7 more
openaire   +3 more sources

The intracellular Ca2+ channel TRPML3 is a PI3P effector that regulates autophagosome biogenesis. [PDF]

open access: yesProc Natl Acad Sci U S A, 2022
Autophagy is a multiple fusion event, initiating with autophagosome formation and culminating with fusion with endo-lysosomes in a Ca 2+ -dependent manner. The source of Ca 2+ and the molecular mechanism by which Ca 2+
Kim SW   +8 more
europepmc   +3 more sources

Cryo-electron microscopy structure of the lysosomal calcium-permeable channel TRPML3 [PDF]

open access: yesNature, 2017
The modulation of ion channel activity by lipids is increasingly recognized as a fundamental component of cellular signalling. The transient receptor potential mucolipin (TRPML) channel family belongs to the TRP superfamily and is composed of three members: TRPML1-TRPML3. TRPMLs are the major Ca2+-permeable channels on late endosomes and lysosomes (LEL)
Marscha, Hirschi   +7 more
openaire   +3 more sources

Neurodegenerative Lysosomal Storage Disorders: TPC2 Comes to the Rescue!

open access: yesCells, 2022
Lysosomal storage diseases (LSDs) resulting from inherited gene mutations constitute a family of disorders that disturb lysosomal degradative function leading to abnormal storage of macromolecular substrates.
Sandra Prat Castro   +5 more
doaj   +1 more source

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