Abstract
CXCR4 (fusin) is a chemokine receptor which is involved as a coreceptor in gp120 binding to the cell surface. In this study we provide evidence that binding of gp120 triggers CXCR4 recruitment to glycosphingolipid-enriched microdomains. Scanning confocal microscopy showed a nearly complete localization of CXCR4 within GM3-enriched plasma membrane domains of SupT1 cells and coimmunoprecipitation experiments revealed that CXCR4 was immunoprecipitated by IgG anti-GM3 after gp120 pretreatment. These findings reveal that gp120 binding induces a strict association between CXCR4 and ganglioside GM3, supporting the view that GM3 and CXCR4 are components of a functional multimolecular complex critical for HIV-1 entry.
| Original language | English |
|---|---|
| Pages (from-to) | 55-60 |
| Number of pages | 6 |
| Journal | FEBS Letters |
| Volume | 506 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Sep 28 2001 |
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Keywords
- CXCR4
- Ganglioside
- GM3
- gp120
- Microdomain
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Evidence for cell surface association between CXCR4 and ganglioside GM3 after gp120 binding in SupT1 lymphoblastoid cells. / Sorice, Maurizio; Garofalo, Tina; Misasi, Roberta; Longo, Agostina; Mattei, Vincenzo; Sale, Patrizio; Dolo, Vincenza; Gradini, Roberto; Pavan, Antonio.
In: FEBS Letters, Vol. 506, No. 1, 28.09.2001, p. 55-60.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Evidence for cell surface association between CXCR4 and ganglioside GM3 after gp120 binding in SupT1 lymphoblastoid cells
AU - Sorice, Maurizio
AU - Garofalo, Tina
AU - Misasi, Roberta
AU - Longo, Agostina
AU - Mattei, Vincenzo
AU - Sale, Patrizio
AU - Dolo, Vincenza
AU - Gradini, Roberto
AU - Pavan, Antonio
PY - 2001/9/28
Y1 - 2001/9/28
N2 - CXCR4 (fusin) is a chemokine receptor which is involved as a coreceptor in gp120 binding to the cell surface. In this study we provide evidence that binding of gp120 triggers CXCR4 recruitment to glycosphingolipid-enriched microdomains. Scanning confocal microscopy showed a nearly complete localization of CXCR4 within GM3-enriched plasma membrane domains of SupT1 cells and coimmunoprecipitation experiments revealed that CXCR4 was immunoprecipitated by IgG anti-GM3 after gp120 pretreatment. These findings reveal that gp120 binding induces a strict association between CXCR4 and ganglioside GM3, supporting the view that GM3 and CXCR4 are components of a functional multimolecular complex critical for HIV-1 entry.
AB - CXCR4 (fusin) is a chemokine receptor which is involved as a coreceptor in gp120 binding to the cell surface. In this study we provide evidence that binding of gp120 triggers CXCR4 recruitment to glycosphingolipid-enriched microdomains. Scanning confocal microscopy showed a nearly complete localization of CXCR4 within GM3-enriched plasma membrane domains of SupT1 cells and coimmunoprecipitation experiments revealed that CXCR4 was immunoprecipitated by IgG anti-GM3 after gp120 pretreatment. These findings reveal that gp120 binding induces a strict association between CXCR4 and ganglioside GM3, supporting the view that GM3 and CXCR4 are components of a functional multimolecular complex critical for HIV-1 entry.
KW - CXCR4
KW - Ganglioside
KW - GM3
KW - gp120
KW - Microdomain
UR - http://www.scopus.com/inward/record.url?scp=0035964926&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035964926&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(01)02830-7
DO - 10.1016/S0014-5793(01)02830-7
M3 - Article
C2 - 11591370
AN - SCOPUS:0035964926
VL - 506
SP - 55
EP - 60
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1
ER -