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Team Publications
Membrane and Cytoskeleton Dynamics
Year of publication 2010
Philippe Chavrier, Julie Ménétrey (2010 Dec 8)
Toward a structural understanding of arf family:effector specificity.
Structure (London, England : 1993) : 1552-8 : DOI : 10.1016/j.str.2010.11.004
Summary
Arf family proteins are critical regulators of intracellular trafficking and actin cytoskeleton
dynamics. To carry out their cellular functions, Arf family proteins interact with various
effectors that differ in nature and structure. Understanding how these proteins interact with
structurally different partners and are distinguished by specific effectors while being closely
related requires a structural characterization and comparison of the various Arf
family:effector complexes. Recent structural reports of Arf and Arl proteins in complex with
different downstream effectors shed new light on general and specific structural recognition
determinants characteristic of Arf family proteins.
Guillaume Montagnac, Hélène de Forges, Elizabeth Smythe, Charles Gueudry, Maryse Romao,
Jean Salamero, Philippe Chavrier (2010 Nov 23)
Decoupling of activation and effector binding underlies ARF6 priming of fast
endocytic recycling.
Current biology : CB : 574-9 : DOI : 10.1016/j.cub.2011.02.034
Summary
The small GTP-binding protein ADP-ribosylation factor 6 (ARF6) controls the endocytic
recycling pathway of several plasma membrane receptors. We analyzed the localization and
GDP/GTP cycle of GFP-tagged ARF6 by total internal reflection fluorescent microscopy. We
found that ARF6-GFP associates with clathrin-coated pits (CCPs) at the plasma membrane in
a GTP-dependent manner in a mechanism requiring the adaptor protein complex AP-2. In
CCP, GTP-ARF6 mediates the recruitment of the ARF-binding domain of downstream effectors
including JNK-interacting proteins 3 and 4 (JIP3 and JIP4) after the burst recruitment of the
clathrin uncoating component auxilin. ARF6 does not contribute to receptor-mediated
clathrin-dependent endocytosis. In contrast, we found that interaction of ARF6 and JIPs on
endocytic vesicles is required for trafficking of the transferrin receptor in the fast,
microtubule-dependent endocytic recycling pathway. Our findings unravel a novel
mechanism of separation of ARF6 activation and effector function, ensuring that fast
recycling may be determined at the level of receptor incorporation into CCPs.
Mercedes Rey, Marie Irondelle, François Waharte, Floria Lizarraga, Philippe Chavrier (2010 Oct
26)
HDAC6 is required for invadopodia activity and invasion by breast tumor cells.
European journal of cell biology : 128-35 : DOI : 10.1016/j.ejcb.2010.09.004
INSTITUT CURIE, 20 rue d’Ulm, 75248 Paris Cedex 05, France | 1
Team Publications
Membrane and Cytoskeleton Dynamics
Summary
Invasion across tissue boundaries by metastatic tumor cells depends on the proteolytic
degradation of the extracellular matrix, initiated by the formation of invadopodia, actindriven membrane protrusions with matrix-degradative activity. Yet, mechanisms underlying
invadopodia formation remain largely unknown. In this report, we examined the role of the
histone deacetylase HDAC6 in invadopodia formation and invasion by breast cancer cells.
Using small interfering RNA silencing of protein expression in highly invasive MDA-MB-231
breast adenocarcinoma cells, we show that HDAC6 is required for two-dimensional matrix
proteolysis. In addition, we demonstrate that HDAC6 acts as a tubulin and cortactin
deacetylase. We also report that the inhibition of HDAC6 by siRNA or treatment with HDAC
inhibitor TSA results in a decreased invasion capacity of a three-dimensional type I collagen
matrix by MDA-MB-231 cells. These data identify HDAC6 as a critical component of the
invasive apparatus of tumor cells, in both two- and three-dimensional matrices.
Guillaume Montagnac, Philippe Chavrier (2010 Apr 3)
Abscission accomplished by PtdIns(3)P.
Nature cell biology : 308-10 : DOI : 10.1038/ncb0410-308
Summary
Cytokinesis – the final step of mitosis in which the two daughter cells separate – requires
accumulation of specific proteins and lipids at the connecting bridge to ensure cleavage by
abscission. Phosphatidylinositol-3-phosphate (PtdIns(3)P), an endosomal phosphoinositide,
and FYVE-CENT, a PtdIns3P-binding protein, are found in the bridge, where they contribute to
the mechanism of abscission.
INSTITUT CURIE, 20 rue d’Ulm, 75248 Paris Cedex 05, France | 2