Scripps VIVO scripps research logo

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

Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation

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

Overview

authors

  • Foisner, R.
  • Gerace, Larry

publication date

  • July 1993

journal

  • Cell  Journal

abstract

  • Lamina-associated polypeptides (LAPs) 1A, 1B, 1C, and 2 are integral membrane proteins of the nuclear envelope associated with the nuclear lamina. Using in vitro assays, we show that LAPs 1A and 1B specifically bind to both lamins A and C and lamin B1, while LAP 2 associates only with lamin B1. LAP 2 also binds to mitotic chromosomes. The LAPs are phosphorylated during mitosis, and phosphorylation of LAP 2 by mitotic cytosol inhibits its binding to both lamin B1 and chromosomes. During late anaphase, LAP 2 associates with chromosomes prior to assembly of most lamins. Together, these data suggest that LAP 2 may have a key role in initial events of nuclear envelope reassembly, and that both LAP 2 and LAP 1 may be involved in attaching lamins to the nuclear envelope.

subject areas

  • Animals
  • Binding Sites
  • CHO Cells
  • Chromosomes
  • Cricetinae
  • Lamin Type B
  • Lamins
  • Liver
  • Membrane Proteins
  • Microsomes
  • Mitosis
  • Nuclear Envelope
  • Nuclear Proteins
  • Phosphorylation
  • Rats
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/0092-8674(93)90355-t

PubMed ID

  • 8324822
scroll to property group menus

Additional Document Info

start page

  • 1267

end page

  • 1279

volume

  • 73

issue

  • 7

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

  • About
  • Contact Us
  • Support