Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+ homeostasis

The internal environment of the ER is regulated to accommodate essential cellular processes, yet our understanding of this regulation remains incomplete. Cod1p/Spf1p belongs to the widely conserved, uncharacterized type V branch of P-type ATPases, a large family of ion pumps. Our previous work sugge...

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Main Authors:	Cronin, Stephen R., Rao, Rajini, Hampton, Randolph Y.
Format:	Online
Language:	English
Published:	The Rockefeller University Press 2002
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174042/

id	pubmed-2174042
recordtype	oai_dc
spelling	pubmed-21740422008-05-01 Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+ homeostasis Cronin, Stephen R. Rao, Rajini Hampton, Randolph Y. Article The internal environment of the ER is regulated to accommodate essential cellular processes, yet our understanding of this regulation remains incomplete. Cod1p/Spf1p belongs to the widely conserved, uncharacterized type V branch of P-type ATPases, a large family of ion pumps. Our previous work suggested Cod1p may function in the ER. Consistent with this hypothesis, we localized Cod1p to the ER membrane. The cod1Δ mutant disrupted cellular calcium homeostasis, causing increased transcription of calcium-regulated genes and a synergistic increase in cellular calcium when paired with disruption of the Golgi apparatus–localized Ca2+ pump Pmr1p. Deletion of COD1 also impaired ER function, causing constitutive activation of the unfolded protein response, hypersensitivity to the glycosylation inhibitor tunicamycin, and synthetic lethality with deletion of the unfolded protein response regulator HAC1. Expression of the Drosophila melanogaster homologue of Cod1p complemented the cod1Δ mutant. Finally, we demonstrated the ATPase activity of the purified protein. This study provides the first biochemical characterization of a type V P-type ATPase, implicates Cod1p in ER function and ion homeostasis, and indicates that these functions are conserved among Cod1p's metazoan homologues. The Rockefeller University Press 2002-06-10 /pmc/articles/PMC2174042/ /pubmed/12058017 http://dx.doi.org/10.1083/jcb.200203052 Text en Copyright © 2002, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Cronin, Stephen R. Rao, Rajini Hampton, Randolph Y.
spellingShingle	Cronin, Stephen R. Rao, Rajini Hampton, Randolph Y. Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+ homeostasis
author_facet	Cronin, Stephen R. Rao, Rajini Hampton, Randolph Y.
author_sort	Cronin, Stephen R.
title	Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+ homeostasis
title_short	Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+ homeostasis
title_full	Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+ homeostasis
title_fullStr	Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+ homeostasis
title_full_unstemmed	Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+ homeostasis
title_sort	cod1p/spf1p is a p-type atpase involved in er function and ca2+ homeostasis
description	The internal environment of the ER is regulated to accommodate essential cellular processes, yet our understanding of this regulation remains incomplete. Cod1p/Spf1p belongs to the widely conserved, uncharacterized type V branch of P-type ATPases, a large family of ion pumps. Our previous work suggested Cod1p may function in the ER. Consistent with this hypothesis, we localized Cod1p to the ER membrane. The cod1Δ mutant disrupted cellular calcium homeostasis, causing increased transcription of calcium-regulated genes and a synergistic increase in cellular calcium when paired with disruption of the Golgi apparatus–localized Ca2+ pump Pmr1p. Deletion of COD1 also impaired ER function, causing constitutive activation of the unfolded protein response, hypersensitivity to the glycosylation inhibitor tunicamycin, and synthetic lethality with deletion of the unfolded protein response regulator HAC1. Expression of the Drosophila melanogaster homologue of Cod1p complemented the cod1Δ mutant. Finally, we demonstrated the ATPase activity of the purified protein. This study provides the first biochemical characterization of a type V P-type ATPase, implicates Cod1p in ER function and ion homeostasis, and indicates that these functions are conserved among Cod1p's metazoan homologues.
publisher	The Rockefeller University Press
publishDate	2002
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174042/
_version_	1611425502337171456

Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+ homeostasis

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