Proliferation of the endoplasmic reticulum occurs normally in cells that lack a functional unfolded protein response

Lynnelle L. Larson, Mark L. Parrish, Ann J. Koning, Robin L. Wright

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Increased expression of certain ER membrane proteins leads to biogenesis of novel ER membrane arrays. These structures provide models in which to explore the mechanisms by which cells control the size and organization of organelles in response to changing physiological demands. In yeast, elevated levels of HMG-CoA reductase induce ER arrays known as karmellae. Cox and co-workers (1997) discovered that karmellae assembly is toxic to ire1 mutants. These mutants are unable to initiate the unfolded protein response, which enables cells to adjust levels of ER chaperones in response to stresses. We sought to determine whether the karmellae-dependent death of ire1 mutants was due to karmellae assembly or to increased levels of HMG-CoA reductase activity. Unexpectedly, we found that ire1 cells could assemble normal levels of karmellae that were structurally identical to those of wild-type cells. In addition, karmellae assembly did not itself induce the unfolded protein response. Certain ire1 strains produced significant numbers of transformants that were unable to utilize galactose as sole carbon source. These results suggest that the karmellae-dependent death of certain ire1 strains may simply reflect their inability to grow on galactose.

Original languageEnglish (US)
Pages (from-to)373-393
Number of pages21
JournalYeast
Volume19
Issue number4
DOIs
StatePublished - Mar 15 2002

Fingerprint

Unfolded Protein Response
Endoplasmic Reticulum
Hydroxymethylglutaryl CoA Reductases
Proteins
Galactose
Membranes
Poisons
Model structures
Cell Size
Organelles
Yeast
Membrane Proteins
Carbon
Yeasts
Oxidoreductases

Keywords

  • ER quality control
  • HMG-CoA reductase
  • IRE1
  • Karmellae
  • Yeast

Cite this

Proliferation of the endoplasmic reticulum occurs normally in cells that lack a functional unfolded protein response. / Larson, Lynnelle L.; Parrish, Mark L.; Koning, Ann J.; Wright, Robin L.

In: Yeast, Vol. 19, No. 4, 15.03.2002, p. 373-393.

Research output: Contribution to journalArticle

Larson, Lynnelle L. ; Parrish, Mark L. ; Koning, Ann J. ; Wright, Robin L. / Proliferation of the endoplasmic reticulum occurs normally in cells that lack a functional unfolded protein response. In: Yeast. 2002 ; Vol. 19, No. 4. pp. 373-393.
@article{33d7f429c6c346e88970221ac38fdaf6,
title = "Proliferation of the endoplasmic reticulum occurs normally in cells that lack a functional unfolded protein response",
abstract = "Increased expression of certain ER membrane proteins leads to biogenesis of novel ER membrane arrays. These structures provide models in which to explore the mechanisms by which cells control the size and organization of organelles in response to changing physiological demands. In yeast, elevated levels of HMG-CoA reductase induce ER arrays known as karmellae. Cox and co-workers (1997) discovered that karmellae assembly is toxic to ire1 mutants. These mutants are unable to initiate the unfolded protein response, which enables cells to adjust levels of ER chaperones in response to stresses. We sought to determine whether the karmellae-dependent death of ire1 mutants was due to karmellae assembly or to increased levels of HMG-CoA reductase activity. Unexpectedly, we found that ire1 cells could assemble normal levels of karmellae that were structurally identical to those of wild-type cells. In addition, karmellae assembly did not itself induce the unfolded protein response. Certain ire1 strains produced significant numbers of transformants that were unable to utilize galactose as sole carbon source. These results suggest that the karmellae-dependent death of certain ire1 strains may simply reflect their inability to grow on galactose.",
keywords = "ER quality control, HMG-CoA reductase, IRE1, Karmellae, Yeast",
author = "Larson, {Lynnelle L.} and Parrish, {Mark L.} and Koning, {Ann J.} and Wright, {Robin L.}",
year = "2002",
month = "3",
day = "15",
doi = "10.1002/yea.839",
language = "English (US)",
volume = "19",
pages = "373--393",
journal = "Yeast",
issn = "0749-503X",
publisher = "John Wiley and Sons Ltd",
number = "4",

}

TY - JOUR

T1 - Proliferation of the endoplasmic reticulum occurs normally in cells that lack a functional unfolded protein response

AU - Larson, Lynnelle L.

AU - Parrish, Mark L.

AU - Koning, Ann J.

AU - Wright, Robin L.

PY - 2002/3/15

Y1 - 2002/3/15

N2 - Increased expression of certain ER membrane proteins leads to biogenesis of novel ER membrane arrays. These structures provide models in which to explore the mechanisms by which cells control the size and organization of organelles in response to changing physiological demands. In yeast, elevated levels of HMG-CoA reductase induce ER arrays known as karmellae. Cox and co-workers (1997) discovered that karmellae assembly is toxic to ire1 mutants. These mutants are unable to initiate the unfolded protein response, which enables cells to adjust levels of ER chaperones in response to stresses. We sought to determine whether the karmellae-dependent death of ire1 mutants was due to karmellae assembly or to increased levels of HMG-CoA reductase activity. Unexpectedly, we found that ire1 cells could assemble normal levels of karmellae that were structurally identical to those of wild-type cells. In addition, karmellae assembly did not itself induce the unfolded protein response. Certain ire1 strains produced significant numbers of transformants that were unable to utilize galactose as sole carbon source. These results suggest that the karmellae-dependent death of certain ire1 strains may simply reflect their inability to grow on galactose.

AB - Increased expression of certain ER membrane proteins leads to biogenesis of novel ER membrane arrays. These structures provide models in which to explore the mechanisms by which cells control the size and organization of organelles in response to changing physiological demands. In yeast, elevated levels of HMG-CoA reductase induce ER arrays known as karmellae. Cox and co-workers (1997) discovered that karmellae assembly is toxic to ire1 mutants. These mutants are unable to initiate the unfolded protein response, which enables cells to adjust levels of ER chaperones in response to stresses. We sought to determine whether the karmellae-dependent death of ire1 mutants was due to karmellae assembly or to increased levels of HMG-CoA reductase activity. Unexpectedly, we found that ire1 cells could assemble normal levels of karmellae that were structurally identical to those of wild-type cells. In addition, karmellae assembly did not itself induce the unfolded protein response. Certain ire1 strains produced significant numbers of transformants that were unable to utilize galactose as sole carbon source. These results suggest that the karmellae-dependent death of certain ire1 strains may simply reflect their inability to grow on galactose.

KW - ER quality control

KW - HMG-CoA reductase

KW - IRE1

KW - Karmellae

KW - Yeast

UR - http://www.scopus.com/inward/record.url?scp=0037087285&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037087285&partnerID=8YFLogxK

U2 - 10.1002/yea.839

DO - 10.1002/yea.839

M3 - Article

VL - 19

SP - 373

EP - 393

JO - Yeast

JF - Yeast

SN - 0749-503X

IS - 4

ER -