Narcissistic CLIP-170 also attracts dynactin
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چکیده
منابع مشابه
Narcissistic CLIP-170 also attracts dynactin
caffolds that hold up membrane proteins in red blood cells also support the channels needed for neuronal signaling, as shown by Lacas-Gervais et al. on page 983. Neurons fire when sodium channels clustered at the axonal initial segment (AIS) open. This depolarization is propagated by more channels clustered along axons in the Nodes of Ranvier (NR). The structure of these compartments is now sho...
متن کاملLIS1, CLIP-170's key to the dynein/dynactin pathway.
CLIP-170 is a plus-end tracking protein which may act as an anticatastrophe factor. It has been proposed to mediate the association of dynein/dynactin to microtubule (MT) plus ends, and it also binds to kinetochores in a dynein/dynactin-dependent fashion, both via its C-terminal domain. This domain contains two zinc finger motifs (proximal and distal), which are hypothesized to mediate protein-...
متن کاملConformational changes in CLIP-170 regulate its binding to microtubules and dynactin localization
Cytoplasmic linker protein (CLIP)-170, CLIP-115, and the dynactin subunit p150(Glued) are structurally related proteins, which associate specifically with the ends of growing microtubules (MTs). Here, we show that down-regulation of CLIP-170 by RNA interference results in a strongly reduced accumulation of dynactin at the MT tips. The NH(2) terminus of p150(Glued) binds directly to the COOH ter...
متن کاملRole of dynein, dynactin, and CLIP-170 interactions in LIS1 kinetochore function
Mutations in the human LIS1 gene cause type I lissencephaly, a severe brain developmental disease involving gross disorganization of cortical neurons. In lower eukaryotes, LIS1 participates in cytoplasmic dynein-mediated nuclear migration. We previously reported that mammalian LIS1 functions in cell division and coimmunoprecipitates with cytoplasmic dynein and dynactin. We also localized LIS1 t...
متن کاملInteractions between CLIP-170, tubulin, and microtubules: implications for the mechanism of Clip-170 plus-end tracking behavior.
CLIP-170 belongs to a group of proteins (+TIPs) with the enigmatic ability to dynamically track growing microtubule plus-ends. CLIP-170 regulates microtubule dynamics in vivo and has been implicated in cargo-microtubule interactions in vivo and in vitro. Though plus-end tracking likely has intimate connections to +TIP function, little is known about the mechanism(s) by which this dynamic locali...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2004
ISSN: 1540-8140,0021-9525
DOI: 10.1083/jcb1667iti4