About: Regulation of V-ATPase Activity and Organelle pH by Phosphatidylinositol Phosphate Lipids

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Regulation of V-ATPase Activity and Organelle pH by Phosphatidylinositol Phosphate Lipids
Creator	Banerjee, Subhrajit Kane, Patricia Stefan, Chris Weisman, Lois
source	Medline; PMC
abstract	Luminal pH and the distinctive distribution of phosphatidylinositol phosphate (PIP) lipids are central identifying features of organelles in all eukaryotic cells that are also critical for organelle function. V-ATPases are conserved proton pumps that populate and acidify multiple organelles of the secretory and the endocytic pathway. Complete loss of V-ATPase activity causes embryonic lethality in higher animals and conditional lethality in yeast, while partial loss of V-ATPase function is associated with multiple disease states. On the other hand, many cancer cells increase their virulence by upregulating V-ATPase expression and activity. The pH of individual organelles is tightly controlled and essential for function, but the mechanisms for compartment-specific pH regulation are not completely understood. There is substantial evidence indicating that the PIP content of membranes influences organelle pH. We present recent evidence that PIPs interact directly with subunit isoforms of the V-ATPase to dictate localization of V-ATPase subpopulations and participate in their regulation. In yeast cells, which have only one set of organelle-specific V-ATPase subunit isoforms, the Golgi-enriched lipid PI(4)P binds to the cytosolic domain of the Golgi-enriched a-subunit isoform Stv1, and loss of PI(4)P binding results in mislocalization of Stv1-containing V-ATPases from the Golgi to the vacuole/lysosome. In contrast, levels of the vacuole/lysosome-enriched signaling lipid PI(3,5)P(2) affect assembly and activity of V-ATPases containing the Vph1 a-subunit isoform. Mutations in the Vph1 isoform that disrupt the lipid interaction increase sensitivity to stress. These studies have decoded “zip codes” for PIP lipids in the cytosolic N-terminal domain of the a-subunit isoforms of the yeast V-ATPase, and similar interactions between PIP lipids and the V-ATPase subunit isoforms are emerging in higher eukaryotes. In addition to direct effects on the V-ATPase, PIP lipids are also likely to affect organelle pH indirectly, through interactions with other membrane transporters. We discuss direct and indirect effects of PIP lipids on organelle pH, and the functional consequences of the interplay between PIP lipid content and organelle pH.
has issue date	2020-06-23(xsd:dateTime)
bibo:doi	10.3389/fcell.2020.00510
bibo:pmid	32656214
has license	cc-by
sha1sum (hex)	b07ceb888f5bd27b99d3277e8f7bc6f73d016925
schema:url	https://doi.org/10.3389/fcell.2020.00510
resource representing a document's title	Regulation of V-ATPase Activity and Organelle pH by Phosphatidylinositol Phosphate Lipids
has PubMed Central identifier	PMC7324685
has PubMed identifier	32656214
schema:publication	Front Cell Dev Biol
resource representing a document's body	covid:b07ceb888f5bd27b99d3277e8f7bc6f73d016925#body_text
is schema:about of	named entity 'conserved' named entity 'direct effects' named entity 'Luminal' named entity 'V-ATPases' named entity 'CONSEQUENCES' named entity 'LOSS OF' named entity 'SIMILAR' named entity 'SET' named entity 'ENDOCYTIC PATHWAY' named entity 'COMPLETE' named entity 'LEVELS' named entity 'HAVE' named entity 'CONTENT' named entity 'THEIR' named entity 'TO DIRECT' named entity 'PH REGULATION' named entity 'LIPID CONTENT' named entity 'INTERACT' named entity 'CONDITIONAL' named entity 'CONTAINING' named entity 'PROTON PUMPS' covid:arg/b07ceb888f5bd27b99d3277e8f7bc6f73d016925 named entity 'decoded' named entity 'partial' named entity 'V-ATPase' named entity 'lipid' named entity 'interactions' named entity 'lipids' named entity 'activity' named entity 'disrupt' named entity 'organelle' named entity 'controlled' named entity 'PIP' named entity 'cytosolic' named entity 'PIP' named entity 'function' named entity 'participate' named entity 'Stv1' named entity 'lysosome' named entity 'eukaryotes' named entity 'PI(4)P' named entity 'V-ATPase' named entity 'isoform' named entity 'organelle' named entity 'vacuole' named entity 'Golgi' named entity 'isoforms' named entity 'organelle' named entity 'V-ATPase' named entity 'virulence' named entity 'lipids' named entity 'isoforms' named entity 'V-ATPase' named entity 'PI(4)P' named entity 'V-ATPase' named entity 'V-ATPase' named entity 'cancer cells' named entity 'organelle' named entity 'lipids' named entity 'isoform' named entity 'organelles' named entity 'organelle' named entity 'V-ATPase' named entity 'Lipids' named entity 'Phosphatidylinositol Phosphate' named entity 'V-ATPase' named entity 'PI(3)P' named entity 'V-ATPase' named entity 'phosphoinositide' named entity 'vacuolation' named entity 'kDa' named entity 'yeast' named entity 'patch clamp' named entity 'autophagy' named entity 'polar amino acid residues' named entity 'protein sequence' named entity 'orthologs' named entity '3,5'

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