Functional diversity of LAP2[alpha] and LAP2[beta] in postmitotic chromosome association is caused by an [alpha]-specific nuclear targeting domain

Lamina-associated polypeptide 2[alpha] (LAP2[alpha]) is a non-membrane-bound isoform of the LAP2 family implicated in nuclear structure organization. We show that during postmitotic nuclear assembly LAP2[alpha] associates with chromosomes prior to accumulation of the membrane-bound isoform LAP2[beta...

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Published in:The EMBO journal 1999-11, Vol.18 (22), p.6370
Main Authors: Vlcek, Sylvia, Just, Herwig, Dechat, Thomas, Foisner, Roland
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Just, Herwig
Dechat, Thomas
Foisner, Roland
description Lamina-associated polypeptide 2[alpha] (LAP2[alpha]) is a non-membrane-bound isoform of the LAP2 family implicated in nuclear structure organization. We show that during postmitotic nuclear assembly LAP2[alpha] associates with chromosomes prior to accumulation of the membrane-bound isoform LAP2[beta], although both proteins contain the same putative chromatin interaction domains located in their common N-terminal regions. By transient and stable expression of various N- and C-terminal LAP2[alpha] deletion mutants in HeLa cells, we identified an ~350-amino-acid-long region in the C-terminal [alpha]-specific domain of the protein that is required for retention of LAP2[alpha] in interphase nuclei and for association with mitotic chromosomes, while the N-terminal domain seemed to be dispensable for these interactions. In vitro chromosome binding studies using recombinant LAP2[alpha] mutants revealed that this LAP2[alpha]-specific 'nuclear targeting domain' was essential and sufficient for association with chromosomes. These data suggested a functional diversity of chromosome binding properties of LAP2 isoforms.
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title Functional diversity of LAP2[alpha] and LAP2[beta] in postmitotic chromosome association is caused by an [alpha]-specific nuclear targeting domain
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