The expression, lamin-dependent localization and RNAi depletion phenotype for emerin in C. elegans

Yosef Gruenbaum, Kenneth K. Lee, Jun Liu, Merav Cohen, Katherine Lee Wilson

Research output: Contribution to journalArticle

Abstract

Emerin belongs to the LEM-domain family of nuclear membrane proteins, which are conserved in metazoans from C. elegans to humans. Loss of emerin in humans causes the X-linked form of Emery-Dreifuss muscular dystrophy (EDMD), but the disease mechanism is not understood. We have begun to address the function of emerin in C. elegans, a genetically tractable nematode. The emerin gene (emr-1) is conserved in C. elegans. We detect Ce-emerin protein in the nuclear envelopes of all cell types except sperm, and find that Ce-emerin co-immunoprecipitates with Ce-lamin from embryo lysates. We show for the first time in any organism that nuclear lamins are essential for the nuclear envelope localization of emerin during early development. We further show that four other types of nuclear envelope proteins, including fellow LEM-domain protein Ce-MAN1, as well as Celamin, UNC-84 and nucleoporins do not depend on Ce-emerin for their localization. This result suggests that emerin is not essential to organize or localize the only lamin (B-type) expressed in C. elegans. We also analyzed the RNAi phenotype resulting from the loss of emerin function in C. elegans under laboratory growth conditions, and found no detectable phenotype throughout development. We propose that C. elegans is an appropriate system in which to study the molecular mechanisms of emerin function in vivo.

Original languageEnglish (US)
Pages (from-to)923-929
Number of pages7
JournalJournal of Cell Science
Volume115
Issue number5
StatePublished - Mar 1 2002

Fingerprint

Lamins
RNA Interference
Phenotype
Nuclear Envelope
Nuclear Proteins
emerin
Emery-Dreifuss Muscular Dystrophy
Lamin Type B
Nuclear Pore Complex Proteins
Muscular Diseases
Spermatozoa
Membrane Proteins
Embryonic Structures

Keywords

  • Emery-Dreifuss muscular dystrophy
  • Lamin
  • Lap2
  • LEM-domain
  • Nuclear envelope

ASJC Scopus subject areas

  • Cell Biology

Cite this

The expression, lamin-dependent localization and RNAi depletion phenotype for emerin in C. elegans. / Gruenbaum, Yosef; Lee, Kenneth K.; Liu, Jun; Cohen, Merav; Wilson, Katherine Lee.

In: Journal of Cell Science, Vol. 115, No. 5, 01.03.2002, p. 923-929.

Research output: Contribution to journalArticle

Gruenbaum, Yosef ; Lee, Kenneth K. ; Liu, Jun ; Cohen, Merav ; Wilson, Katherine Lee. / The expression, lamin-dependent localization and RNAi depletion phenotype for emerin in C. elegans. In: Journal of Cell Science. 2002 ; Vol. 115, No. 5. pp. 923-929.
@article{cfcc120dbf1c4fa895c223558c5cb562,
title = "The expression, lamin-dependent localization and RNAi depletion phenotype for emerin in C. elegans",
abstract = "Emerin belongs to the LEM-domain family of nuclear membrane proteins, which are conserved in metazoans from C. elegans to humans. Loss of emerin in humans causes the X-linked form of Emery-Dreifuss muscular dystrophy (EDMD), but the disease mechanism is not understood. We have begun to address the function of emerin in C. elegans, a genetically tractable nematode. The emerin gene (emr-1) is conserved in C. elegans. We detect Ce-emerin protein in the nuclear envelopes of all cell types except sperm, and find that Ce-emerin co-immunoprecipitates with Ce-lamin from embryo lysates. We show for the first time in any organism that nuclear lamins are essential for the nuclear envelope localization of emerin during early development. We further show that four other types of nuclear envelope proteins, including fellow LEM-domain protein Ce-MAN1, as well as Celamin, UNC-84 and nucleoporins do not depend on Ce-emerin for their localization. This result suggests that emerin is not essential to organize or localize the only lamin (B-type) expressed in C. elegans. We also analyzed the RNAi phenotype resulting from the loss of emerin function in C. elegans under laboratory growth conditions, and found no detectable phenotype throughout development. We propose that C. elegans is an appropriate system in which to study the molecular mechanisms of emerin function in vivo.",
keywords = "Emery-Dreifuss muscular dystrophy, Lamin, Lap2, LEM-domain, Nuclear envelope",
author = "Yosef Gruenbaum and Lee, {Kenneth K.} and Jun Liu and Merav Cohen and Wilson, {Katherine Lee}",
year = "2002",
month = "3",
day = "1",
language = "English (US)",
volume = "115",
pages = "923--929",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "Company of Biologists Ltd",
number = "5",

}

TY - JOUR

T1 - The expression, lamin-dependent localization and RNAi depletion phenotype for emerin in C. elegans

AU - Gruenbaum, Yosef

AU - Lee, Kenneth K.

AU - Liu, Jun

AU - Cohen, Merav

AU - Wilson, Katherine Lee

PY - 2002/3/1

Y1 - 2002/3/1

N2 - Emerin belongs to the LEM-domain family of nuclear membrane proteins, which are conserved in metazoans from C. elegans to humans. Loss of emerin in humans causes the X-linked form of Emery-Dreifuss muscular dystrophy (EDMD), but the disease mechanism is not understood. We have begun to address the function of emerin in C. elegans, a genetically tractable nematode. The emerin gene (emr-1) is conserved in C. elegans. We detect Ce-emerin protein in the nuclear envelopes of all cell types except sperm, and find that Ce-emerin co-immunoprecipitates with Ce-lamin from embryo lysates. We show for the first time in any organism that nuclear lamins are essential for the nuclear envelope localization of emerin during early development. We further show that four other types of nuclear envelope proteins, including fellow LEM-domain protein Ce-MAN1, as well as Celamin, UNC-84 and nucleoporins do not depend on Ce-emerin for their localization. This result suggests that emerin is not essential to organize or localize the only lamin (B-type) expressed in C. elegans. We also analyzed the RNAi phenotype resulting from the loss of emerin function in C. elegans under laboratory growth conditions, and found no detectable phenotype throughout development. We propose that C. elegans is an appropriate system in which to study the molecular mechanisms of emerin function in vivo.

AB - Emerin belongs to the LEM-domain family of nuclear membrane proteins, which are conserved in metazoans from C. elegans to humans. Loss of emerin in humans causes the X-linked form of Emery-Dreifuss muscular dystrophy (EDMD), but the disease mechanism is not understood. We have begun to address the function of emerin in C. elegans, a genetically tractable nematode. The emerin gene (emr-1) is conserved in C. elegans. We detect Ce-emerin protein in the nuclear envelopes of all cell types except sperm, and find that Ce-emerin co-immunoprecipitates with Ce-lamin from embryo lysates. We show for the first time in any organism that nuclear lamins are essential for the nuclear envelope localization of emerin during early development. We further show that four other types of nuclear envelope proteins, including fellow LEM-domain protein Ce-MAN1, as well as Celamin, UNC-84 and nucleoporins do not depend on Ce-emerin for their localization. This result suggests that emerin is not essential to organize or localize the only lamin (B-type) expressed in C. elegans. We also analyzed the RNAi phenotype resulting from the loss of emerin function in C. elegans under laboratory growth conditions, and found no detectable phenotype throughout development. We propose that C. elegans is an appropriate system in which to study the molecular mechanisms of emerin function in vivo.

KW - Emery-Dreifuss muscular dystrophy

KW - Lamin

KW - Lap2

KW - LEM-domain

KW - Nuclear envelope

UR - http://www.scopus.com/inward/record.url?scp=0036500323&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036500323&partnerID=8YFLogxK

M3 - Article

VL - 115

SP - 923

EP - 929

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

IS - 5

ER -