Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control membrane traffic in cytokinesis
AU - Schonteich, Eric
AU - Fielding, Andrew B.
AU - Matheson, Johanne
AU - Wilson, Gayle
AU - Yu, Xinzi
AU - Hickson, Gilles R X
AU - Srivastava, Sweta
AU - Baldwin, Stephen A
AU - Prekeris, Rytis
AU - Gould, Gwyn W
PY - 2005/10/5
Y1 - 2005/10/5
N2 - The dual Rab11/Arf binding proteins, family of Rab11-interacting proteins FIP3 and FIP4 function in the delivery of recycling endosomes to the cleavage furrow and are, together with Rab11, essential for completion of abscission, the terminal step of cytokinesis. Here, we report that both FIP3 and FIP4 bind Arf6 in a nucleotide-dependent manner but exhibit differential affinities for Rab11 and Arf6. Both FIP3 and FIP4 can form ternary complexes with Rab11 and Arf6. Arf6 is localised to the furrow and midbody and we show that Arf6-GTP functions to localise FIP3 and FIP4 to midbodies during cytokinesis. Exo70p, a component of the Exocyst complex, also localises to the furrow of dividing cells and interacts with Arf6. We show that depletion of Exo70p leads to cytokinesis failure and an impairment of FIP3 and Rab11 localisation to the furrow and midbody. Moreover, Exo70p co-immunoprecipitates FIP3 and FIP4. Hence, we propose that FIP3 and FIP4 serve to couple Rab11-positive vesicle traffic from recycling endosomes to the cleavage furrow/midbody where they are tethered prior to fusion events via interactions with Arf6 and the Exocyst.
AB - The dual Rab11/Arf binding proteins, family of Rab11-interacting proteins FIP3 and FIP4 function in the delivery of recycling endosomes to the cleavage furrow and are, together with Rab11, essential for completion of abscission, the terminal step of cytokinesis. Here, we report that both FIP3 and FIP4 bind Arf6 in a nucleotide-dependent manner but exhibit differential affinities for Rab11 and Arf6. Both FIP3 and FIP4 can form ternary complexes with Rab11 and Arf6. Arf6 is localised to the furrow and midbody and we show that Arf6-GTP functions to localise FIP3 and FIP4 to midbodies during cytokinesis. Exo70p, a component of the Exocyst complex, also localises to the furrow of dividing cells and interacts with Arf6. We show that depletion of Exo70p leads to cytokinesis failure and an impairment of FIP3 and Rab11 localisation to the furrow and midbody. Moreover, Exo70p co-immunoprecipitates FIP3 and FIP4. Hence, we propose that FIP3 and FIP4 serve to couple Rab11-positive vesicle traffic from recycling endosomes to the cleavage furrow/midbody where they are tethered prior to fusion events via interactions with Arf6 and the Exocyst.
KW - ADP-Ribosylation Factors
KW - Carrier Proteins
KW - Cell Line, Tumor
KW - Cell Membrane
KW - Cytokinesis
KW - Endocytosis
KW - Endosomes
KW - GTP Phosphohydrolases
KW - Humans
KW - I-kappa B Kinase
KW - Immunoprecipitation
KW - Models, Biological
KW - Multiprotein Complexes
KW - Protein Binding
KW - RNA Interference
KW - rab GTP-Binding Proteins
KW - Comparative Study
KW - Journal Article
KW - Research Support, N.I.H., Extramural
KW - Research Support, U.S. Gov't, P.H.S.
U2 - 10.1038/sj.emboj.7600803
DO - 10.1038/sj.emboj.7600803
M3 - Journal article
C2 - 16148947
VL - 24
SP - 3389
EP - 3399
JO - EMBO Journal
JF - EMBO Journal
SN - 0261-4189
IS - 19
ER -