Rac1 and Cdc42 Capture Microtubules through IQGAP1 and CLIP-170

@article{Fukata2002Rac1AC,
  title={Rac1 and Cdc42 Capture Microtubules through IQGAP1 and CLIP-170},
  author={Masaki Fukata and Takashi Watanabe and Jun Noritake and Masato Nakagawa and Masaki Yamaga and Shinya Kuroda and Yoshiharu Matsuura and Akihiro Iwamatsu and Franck Perez and Kozo Kaibuchi},
  journal={Cell},
  year={2002},
  volume={109},
  pages={873-885}
}
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Mechanistic studies reveal that ASK1-mediated phosphorylation of EB1 enhances the localization of cytoplasmic linker protein 170 (CLIP-170) and p150glued to the plus ends of astral microtubules, thereby recruiting these +TIPs to microtubule plus ends.
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Spatial regulation of CLASP affinity for microtubules by Rac1 and GSK3β in migrating epithelial cells
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References

SHOWING 1-10 OF 117 REFERENCES
CLASPs Are CLIP-115 and -170 Associating Proteins Involved in the Regional Regulation of Microtubule Dynamics in Motile Fibroblasts
CLIP-170 links endocytic vesicles to microtubules
Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1
TLDR
Results indicate that mDia1 may coordinate microtubules and F-actin through its FH2 and FH1 regions, respectively.
IQGAP1, a Rac- and Cdc42-binding Protein, Directly Binds and Cross-links Microfilaments
TLDR
The purification and characterization of a protein, IQGAP1, is reported, which is likely to mediate effects of these GTPases on microfilament-rich lamellipodia and filopodia, and it is suggested that the actin-binding activity of IQG AP1 is regulated by calmodulin.
CLIP-170 Highlights Growing Microtubule Ends In Vivo
mDia mediates Rho-regulated formation and orientation of stable microtubules
TLDR
The results show that mDia is sufficient to generate and orient stable microtubules, and indicate that Dia-related formins are part of a conserved pathway that regulates the dynamics of microtubule ends.
CLIP170-like tip1p Spatially Organizes Microtubular Dynamics in Fission Yeast
Regulation of Cross-linking of Actin Filament by IQGAP1, a Target for Cdc42*
TLDR
Results strongly suggest that IQGAP1, acting downstream of Cdc42, can cross-link the actin filament through its oligomerization.
Colocalization of cytoplasmic dynein with dynactin and CLIP-170 at microtubule distal ends.
TLDR
The functional interaction between dynactin and cytoplasmic dynein further suggests that this these regions represent accumulations of cy toplasmo-dynein cargo-loading sites involved in the early stages of minus end-directed organelle transport.
The dynamic behavior of the APC-binding protein EB1 on the distal ends of microtubules
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