INF1 is a novel microtubule-associated formin

Formin proteins, characterized by the presence of conserved formin homology (FH) domains, play important roles in cytoskeletal regulation via their abilities to nucleate actin filament formation and to interact with multiple other proteins involved in cytoskeletal regulation. The C-terminal FH2 doma...

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Bibliographic Details
Published in:Molecular biology of the cell 2008-12, Vol.19 (12), p.5168-5180
Main Authors: Young, Kevin G, Thurston, Susan F, Copeland, Sarah, Smallwood, Chelsea, Copeland, John W
Format: Article
Language:English
Subjects:
Actins - metabolism
Amino Acid Sequence
Animals
Bridged Bicyclo Compounds, Heterocyclic - metabolism
Cell Line
Cytoskeleton - metabolism
Enzyme Activation
Fetal Proteins - genetics
Fetal Proteins - metabolism
Humans
Mice
Microfilament Proteins - genetics
Microfilament Proteins - metabolism
Microtubule-Associated Proteins - classification
Microtubule-Associated Proteins - genetics
Microtubule-Associated Proteins - metabolism
Microtubules - metabolism
Microtubules - ultrastructure
Molecular Sequence Data
Nocodazole - metabolism
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Phylogeny
Protein Kinases - genetics
Protein Kinases - metabolism
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
RNA, Small Interfering - genetics
RNA, Small Interfering - metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Thiazolidines - metabolism
Tissue Distribution
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Summary:Formin proteins, characterized by the presence of conserved formin homology (FH) domains, play important roles in cytoskeletal regulation via their abilities to nucleate actin filament formation and to interact with multiple other proteins involved in cytoskeletal regulation. The C-terminal FH2 domain of formins is key for actin filament interactions and has been implicated in playing a role in interactions with microtubules. Inverted formin 1 (INF1) is unusual among the formin family in having the conserved FH1 and FH2 domains in its N-terminal half, with its C-terminal half being composed of a unique polypeptide sequence. In this study, we have examined a potential role for INF1 in regulating microtubule structure. INF1 associates discretely with microtubules, and this association is dependent on a novel C-terminal microtubule-binding domain. INF1 expressed in fibroblast cells induced actin stress fiber formation, coalignment of microtubules with actin filaments, and the formation of bundled, acetylated microtubules. Endogenous INF1 showed an association with acetylated microtubules, and knockdown of INF1 resulted in decreased levels of acetylated microtubules. Our data suggests a role for INF1 in microtubule modification and potentially in coordinating microtubule and F-actin structure.
ISSN:1059-1524
1939-4586
DOI:10.1091/mbc.E08-05-0469