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HIV-1 Nef mimics an integrin receptor signal that recruits the polycomb group protein Eed to the plasma membrane

Witte, V ; Laffert, B ; Rosorius, O ; Lischka, P ; Blume, K ; Galler, G ; Stilper, A ; Willbold, D ; D'Aloja, P and Sixt, Michael LU , et al. (2004) In Molecular Cell 13(2). p.179-190
Abstract
The Nef protein of human and simian immunodeficiency virus (HIV/SIV) is believed to interfere with T cell activation signals by forming a signaling complex at the plasma membrane. Composition and function of the complex are not fully understood. Here we report that Nef recruits the Polycomb Group (PcG) protein Eed, so far known as a nuclear factor and repressor of transcription, to the membrane of cells. The Nef-induced translocation of Eed led to a potent stimulation of Tat-dependent HIV transcription, implying that Eed removal from the nucleus is required for optimal Tat function. Similar to Nef action, activation of integrin receptors recruited Eed to the plasma membrane, also leading to enhanced Tat/Nef-mediated transcription. Our... (More)
The Nef protein of human and simian immunodeficiency virus (HIV/SIV) is believed to interfere with T cell activation signals by forming a signaling complex at the plasma membrane. Composition and function of the complex are not fully understood. Here we report that Nef recruits the Polycomb Group (PcG) protein Eed, so far known as a nuclear factor and repressor of transcription, to the membrane of cells. The Nef-induced translocation of Eed led to a potent stimulation of Tat-dependent HIV transcription, implying that Eed removal from the nucleus is required for optimal Tat function. Similar to Nef action, activation of integrin receptors recruited Eed to the plasma membrane, also leading to enhanced Tat/Nef-mediated transcription. Our results suggest a link between membrane-associated activation processes and transcriptional derepression and demonstrate how HIV exploits this mechanism. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Cell
volume
13
issue
2
pages
179 - 190
publisher
Cell Press
external identifiers
  • wos:000188797700003
  • pmid:14759364
  • scopus:10744228109
ISSN
1097-4164
DOI
10.1016/S1097-2765(04)00004-8
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Pathology, (Lund) (013030000)
id
98efcc02-e882-45f5-875d-33856d52b263 (old id 288209)
date added to LUP
2016-04-01 12:11:29
date last changed
2022-03-28 21:29:30
@article{98efcc02-e882-45f5-875d-33856d52b263,
  abstract     = {{The Nef protein of human and simian immunodeficiency virus (HIV/SIV) is believed to interfere with T cell activation signals by forming a signaling complex at the plasma membrane. Composition and function of the complex are not fully understood. Here we report that Nef recruits the Polycomb Group (PcG) protein Eed, so far known as a nuclear factor and repressor of transcription, to the membrane of cells. The Nef-induced translocation of Eed led to a potent stimulation of Tat-dependent HIV transcription, implying that Eed removal from the nucleus is required for optimal Tat function. Similar to Nef action, activation of integrin receptors recruited Eed to the plasma membrane, also leading to enhanced Tat/Nef-mediated transcription. Our results suggest a link between membrane-associated activation processes and transcriptional derepression and demonstrate how HIV exploits this mechanism.}},
  author       = {{Witte, V and Laffert, B and Rosorius, O and Lischka, P and Blume, K and Galler, G and Stilper, A and Willbold, D and D'Aloja, P and Sixt, Michael and Kolanus, J and Ott, M and Kolanus, W and Schuler, G and Baur, AS}},
  issn         = {{1097-4164}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{179--190}},
  publisher    = {{Cell Press}},
  series       = {{Molecular Cell}},
  title        = {{HIV-1 Nef mimics an integrin receptor signal that recruits the polycomb group protein Eed to the plasma membrane}},
  url          = {{http://dx.doi.org/10.1016/S1097-2765(04)00004-8}},
  doi          = {{10.1016/S1097-2765(04)00004-8}},
  volume       = {{13}},
  year         = {{2004}},
}