Cryptic no longer: arrays of CLASP1 TOG domains.
نویسندگان
چکیده
CLASP proteins play crucial roles in regulating microtubules. In this issue of Structure, Leano and colleagues show that an essential and previously cryptic domain of CLASP is a TOG domain with unusual features that might explain its unique functions.
منابع مشابه
A cryptic TOG domain with a distinct architecture underlies CLASP-dependent bipolar spindle formation.
CLASP is a key regulator of microtubule (MT) dynamics and bipolar mitotic spindle structure with CLASP mutants displaying a distinctive monopolar spindle phenotype. It has been postulated that cryptic TOG domains underlie CLASP’s ability to regulate MT dynamics. Here, we report the crystal structure of a cryptic TOG domain (TOG2) from human CLASP1, demonstrating the presence of a TOG array in t...
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متن کاملXMAP215 polymerase activity is built by combining multiple tubulin-binding TOG domains and a basic lattice-binding region.
XMAP215/Dis1 family proteins positively regulate microtubule growth. Repeats at their N termini, called TOG domains, are important for this function. While TOG domains directly bind tubulin dimers, it is unclear how this interaction translates to polymerase activity. Understanding the functional roles of TOG domains is further complicated by the fact that the number of these domains present in ...
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عنوان ژورنال:
- Structure
دوره 21 6 شماره
صفحات -
تاریخ انتشار 2013