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Functions of nuclear inner membrane ...

Lee, Kenneth K.

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Functions of nuclear inner membrane proteins in humans and Caenorhabditis elegans.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Functions of nuclear inner membrane proteins in humans and Caenorhabditis elegans./
Author:	Lee, Kenneth K.
Description:	218 p.
Notes:	Adviser: Katherine L. Wilson.
Contained By:	Dissertation Abstracts International63-03B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3046491
ISBN:	0493606815

Functions of nuclear inner membrane proteins in humans and Caenorhabditis elegans.
Lee, Kenneth K.

Functions of nuclear inner membrane proteins in humans and Caenorhabditis elegans. - 218 p.

Adviser: Katherine L. Wilson.

Thesis (Ph.D.)--The Johns Hopkins University, 2002.

Proteins of the inner nuclear membrane are fundamentally important for nuclear structure and function. Three such proteins, named LAP2, emerin and MAN1, share the 43-residue ‘LEM’ domain. Loss of emerin causes Emery-Dreifuss muscular dystrophy (EDMD), in humans, through unknown mechanisms. To understand this disease, I characterized the functions of human emerin. I first tested the hypothesis that emerin binds barrier-to-autointegration factor (BAF), an essential, conserved DNA-bridging protein in multicellular eukaryotes, with potential roles in nuclear assembly and chromatin organization. Binding was tested biochemically, and domains mapped using 17 alanine-substitution mutants of emerin. This work identified two functional domains in human emerin: the LEM-domain, which is required to bind BAF, and a central domain required to bind lamin A. These results are significant; they suggest that BAF is a binding partner for all LEM-domain proteins, and led me to discover that two disease-causing mutations map outside the BAF- and lamin A-binding regions, potentially defining additional or unique functional domains in emerin that relate directly to the EDMD disease mechanism. I also used <italic>C. elegans </italic> to determine if emerin function is conserved in a genetically tractable system. After identifying and cloning the three LEM-domain genes in <italic> C. elegans</italic>, I showed that the biochemical properties, localization and loss-of-function phenotype of <italic>C. elegans</italic> emerin parallel human emerin. I am currently determining which biochemical functions of human emerin are shared with <italic>C. elegans</italic> emerin, for future genetic analysis of emerin function.

ISBN: 0493606815Subjects--Topical Terms:

1017686
Biology, Cell.

Functions of nuclear inner membrane proteins in humans and Caenorhabditis elegans.
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100 1 $a Lee, Kenneth K. $3 1007934
245 1 0 $a Functions of nuclear inner membrane proteins in humans and Caenorhabditis elegans.
300 $a 218 p.
500 $a Adviser: Katherine L. Wilson.
500 $a Source: Dissertation Abstracts International, Volume: 63-03, Section: B, page: 1121.
502 $a Thesis (Ph.D.)--The Johns Hopkins University, 2002.
520 $a Proteins of the inner nuclear membrane are fundamentally important for nuclear structure and function. Three such proteins, named LAP2, emerin and MAN1, share the 43-residue ‘LEM’ domain. Loss of emerin causes Emery-Dreifuss muscular dystrophy (EDMD), in humans, through unknown mechanisms. To understand this disease, I characterized the functions of human emerin. I first tested the hypothesis that emerin binds barrier-to-autointegration factor (BAF), an essential, conserved DNA-bridging protein in multicellular eukaryotes, with potential roles in nuclear assembly and chromatin organization. Binding was tested biochemically, and domains mapped using 17 alanine-substitution mutants of emerin. This work identified two functional domains in human emerin: the LEM-domain, which is required to bind BAF, and a central domain required to bind lamin A. These results are significant; they suggest that BAF is a binding partner for all LEM-domain proteins, and led me to discover that two disease-causing mutations map outside the BAF- and lamin A-binding regions, potentially defining additional or unique functional domains in emerin that relate directly to the EDMD disease mechanism. I also used <italic>C. elegans </italic> to determine if emerin function is conserved in a genetically tractable system. After identifying and cloning the three LEM-domain genes in <italic> C. elegans</italic>, I showed that the biochemical properties, localization and loss-of-function phenotype of <italic>C. elegans</italic> emerin parallel human emerin. I am currently determining which biochemical functions of human emerin are shared with <italic>C. elegans</italic> emerin, for future genetic analysis of emerin function.
590 $a School code: 0098.
650 4 $a Biology, Cell. $3 1017686
690 $a 0379
710 2 0 $a The Johns Hopkins University. $3 1017431
773 0 $t Dissertation Abstracts International $g 63-03B.
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790 1 0 $a Wilson, Katherine L., $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3046491