QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online 1 April 2003
doi: 10.1242/jcs.00402

This Article Figures Only Full Text Full Text (PDF) All Versions of this Article: jcs.00402v1 116/10/2067    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Mani, S. S. Articles by Wolfner, M. F. Search for Related Content PubMed PubMed Citation Articles by Mani, S. S. Articles by Wolfner, M. F. Social Bookmarking                         What's this?

A hydrophilic lamin-binding domain from the Drosophila YA protein can target proteins to the nuclear envelope

Shobana S. Mani^*, Rithwick Rajagopal, Amanda B. Garfinkel, Xiaochun Fan and Mariana F. Wolfner

Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853-2703, USA
^* Present address: Department of Ophthalmology, SUNY Upstate Medical University, Syracuse, NY13210, USA
Present address: Skirball Institute of Biomolecular Medicine, New York University, New York City, NY 10016, USA

Author for correspondence (e-mail: mfw5{at}cornell.edu)

Accepted 30 January 2003

The nuclear lamina provides an architectural framework for the nuclear envelope and an attachment site for interphase chromatin. In Drosophila eggs and early embryos its major constituent, lamin Dm₀, interacts with a lamina protein called YA. When the lamin-interaction region of YA is deleted, YA still enters nuclei but fails to localize to nuclear envelopes, suggesting that lamin interaction targets YA to the nuclear envelope. Here, we show that C-terminal lamin-interacting region of YA is sufficient to target the heterologous soluble protein GFP-NLS to the nuclear periphery in Drosophila tissue culture cells. Yeast two-hybrid analysis and transient transfection assays further defined this domain: residues 556-696 of YA are sufficient for both lamin Dm₀ interaction and the targeting of GFP-NLS to the nuclear periphery. This region of YA is hydrophilic and lacks any transmembrane domain or known membrane-targeting motifs. We propose that the localization of YA to the nuclear lamina involves interaction with polymerized lamin Dm₀ mediated by the lamin-targeting domain of YA. This hydrophilic YA domain might provide a useful molecular tool for targeting heterologous non-membrane-associated proteins to the nuclear envelope.

Key words: Nuclear lamina, Targeting, Yeast two-hybrid, Drosophila cell transfection, GFP fusion

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?