WebCytoplasmic linker protein 170 (CLIP-170) is a microtubule plus-end factor that links vesicles to microtubules and recruits the dynein–dynactin complex to microtubule plus ends. CLIP-170 plus-end localization is end binding 1 (EB1)–dependent. CLIP-170 contains two N-terminal cytoskeleton-associated protein glycine-rich (CAP-Gly) domains flanked by … WebCytoplasmic linker protein 170 (CLIP-170) is the prototype microtubule (MT) plus-end tracking protein (+TIP) and is involved in regulating MT dynamics. A comprehensive understanding of the...
cytoplasmic linker protein CLIP-170 is a human autoantigen
WebThe cytoplasmic linker protein-170 (CLIP-170) was the first TIP identified (9, 10). Subsequently, numerous structurally unrelated TIP proteins have been iden-tified that are evolutionarily conserved in most eukaryotes. Genetic and biochemical studies have revealed that … WebJun 2, 2010 · Cytoplasmic linker protein (CLIP)-170 is a microtubule (MT) plus-end-tracking protein that regulates MT dynamics and links MT plus ends to different intracellular structures. We have shown previously that … ray wright rocklin
Mapping multivalency in the CLIP-170-EB1 microtubule …
WebSep 14, 2024 · The first identified + TIP protein was cytoplasmic linker protein 170 (CLIP-170). It participates in binding endocytic vesicles to microtubules (Folker et al., 2005). This + TIP protein has CAP-Gly domains that potentially bind to C-terminal EEY motifs, as present in the α-tubulin acidic tail and another + TIP protein, EB1 (Chen L. et al., 2024). WebHerein, we show that the microtubule-binding protein CLIP-170 (cytoplasmic linker protein of 170 kDa) is highly expressed in breast tumor samples and correlates positively with blood vessel density. Depletion of CLIP-170 significantly impaired vascular endothelial tube formation and sprouting in vitro and inhibited breast tumor growth in mice ... WebCytoplasmic linker protein 170 (CLIP-170) is a microtubule (MT) plus-end tracking protein (+ TIP) that dynamically localizes to the MT plus end and regulates MT dynamics. The mechanisms of these activities remain unclear because the CLIP-170-MT interaction is poorly understood, and even less is known about how CLIP-170 and other + TIPs act ... ray wroten maryland