Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Schirmer, E. C.
  • Guan, T. L.
  • Gerace, Larry

publication date

  • April 2001

journal

  • Journal of Cell Biology  Journal

abstract

  • The nuclear lamina is a meshwork of intermediate-type filament proteins (lamins) that lines the inner nuclear membrane. The lamina is proposed to be an important determinant of nuclear structure, but there has been little direct testing of this idea. To investigate lamina functions, we have characterized a novel lamin B1 mutant lacking the middle approximately 4/5 of its alpha-helical rod domain. Though retaining only 10 heptads of the rod, this mutant assembles into intermediate filament-like structures in vitro. When expressed in cultured cells, it concentrates in patches at the nuclear envelope. Concurrently, endogenous lamins shift from a uniform to a patchy distribution and lose their complete colocalization, and nuclei become highly lobulated. In vitro binding studies suggest that the internal rod region is important for heterotypic associations of lamin B1, which in turn are required for proper organization of the lamina. Accompanying the changes in lamina structure induced by expression of the mutant, nuclear pore complexes and integral membrane proteins of the inner membrane cluster, principally at the patches of endogenous lamins. Considered together, these data indicate that lamins play a major role in organizing other proteins in the nuclear envelope and in determining nuclear shape.

subject areas

  • Animals
  • COS Cells
  • Cell Nucleus
  • HeLa Cells
  • Humans
  • Intermediate Filament Proteins
  • Intermediate Filaments
  • Lamin Type B
  • Lamins
  • Mutation
  • Nuclear Envelope
  • Nuclear Pore
  • Nuclear Proteins
  • Protein Binding
  • Protein Engineering
  • Protein Structure, Tertiary
  • Recombinant Proteins
  • Sequence Deletion
scroll to property group menus

Research

keywords

  • intermediate filament
  • lamina-associated polypeptide
  • nuclear lamina
  • nuclear pore complex
  • nuclear shape
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.153.3.479

PubMed ID

  • 11331300
scroll to property group menus

Additional Document Info

start page

  • 479

end page

  • 489

volume

  • 153

issue

  • 3

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support