The Human Mutation K237_V238del in a Putative Lipid Binding Motif within the V-ATPase a2 Isoform Suggests a Molecular Mechanism Underlying Cutis Laxa

The Human Mutation K237_V238del in a Putative Lipid Binding Motif within the V-ATPase a2 Isoform Suggests a Molecular Mechanism Underlying Cutis Laxa

Vacuolar ATPases (V-ATPases), proton pumps composed of 16 subunits, are necessary for a variety of cellular functions. Subunit “a” has four isoforms, a1–a4, each with a distinct cellular location. We identified a phosphoinositide (PIP) interaction motif, KX<sub>n</sub>K(R)IK(R), conserve...

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Bibliographic Details
Main Authors: Anh Chu, Yeqi Yao, Miroslawa Glibowicka, Charles M. Deber, Morris F. Manolson
Format: Article
Language:English
Published: MDPI AG 2024-02-01
Series:International Journal of Molecular Sciences
Subjects:
V-ATPases
V-ATPase a2 isoforms
protein–lipid interaction
phosphoinositides
PI(4)P
cutis laxa
Online Access:https://www.mdpi.com/1422-0067/25/4/2170

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