The giant protein HERC1 is recruited to aluminum fluoride‐induced actin‐rich surface protrusions in HeLa cells

FEBS Letters

Bartrons, Ramon²  Casaroli-Marano, Ricardo P¹  Garcia-Gonzalo, Francesc R²  González, Elena²  Ventura, Francesc²  Muñoz, Purificación²  Rosa, Jose Luis²  Vilaró, Senén¹ 

[1] Departament de Biologia Cellular, Universitat de Barcelona, E-08028 Barcelona, Spain;Departament de Ciències Fisiològiques II, Campus de Bellvitge, Universitat de Barcelona, E-08907 L'Hospitalet de Llobregat, Barcelona, Spain

关键词: HERC1;    Aluminum fluoride;    ARF6;    Phosphoinositide;    Actin protrusion;    Guanine nucleotide exchange factor;    GEF;    guanine nucleotide exchange factor;    FITC;    fluorescein isothiocyanate;    TRITC;    Texas red isothiocyanate;    GFP;    green fluorescent protein;   

DOI  :  10.1016/S0014-5793(04)00030-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

HERC1 is a very large protein involved in membrane traffic through both its ability to bind clathrin and its guanine nucleotide exchange factor (GEF) activity over ARF and Rab family GTPases. Herein, we show that HERC1 is recruited onto actin-rich surface protrusions in ARF6-transfected HeLa cells upon aluminum fluoride (AlF₄ ⁻) treatment. Moreover, the fact that HERC1 overexpression does not stimulate protrusion formation in the absence of AlF₄ ⁻, in conditions where ARNO does, indicates that HERC1 is not acting as an ARF6-GEF in this system, but that instead its recruitment takes place downstream of ARF6 activation. Finally, we suggest a phosphoinositide-binding mechanism whereby HERC1 may translocate to these protrusions.

【 授权许可】

Unknown