منابع مشابه
Glued to microtubule plus ends in organelle transport
subset of microtubule-associated proteins, including cytoplasmic linker protein (CLIP)-170, dynactin, EB1, adenomatous polyposis coli, cytoplasmic dynein, CLASPs, and LIS-1, has been shown recently to target to the plus ends of microtubules. The mechanisms and functions of this binding specificity are not understood, although a role in encouraging microtubule elongation has been proposed. To ex...
متن کاملQuick hops on and off plus ends
A newly identifi ed traffi cking pathway takes a cell surface protein to the inner nuclear membrane (INM), reveal Hieda et al. In its nuclear envelope locale, the protein can reactivate cell cycle genes. Activation of the cell cycle is an important job for EGF family members. These trans-membrane proteins start out on the plasma membrane but are cleaved when cells receive mitogenic cues, thereb...
متن کاملOn Ends-to-Ends Encryption
In the past few years secure messaging has become mainstream, with over a billion active users of end-to-end encryption protocols through apps such as WhatsApp, Signal, Facebook Messenger, Google Allo, Wire and many more. While these users’ two-party communications now enjoy very strong security guarantees, it turns out that many of these apps provide, without notifying the users, a weaker prop...
متن کاملDynamic Localization of CLIP-170 to Microtubule Plus Ends Is Coupled to Microtubule Assembly
CLIP-170 is a cytoplasmic linker protein that localizes to plus ends of microtubules in vivo. In this study, we have characterized the microtubule-binding properties of CLIP-170, to understand the mechanism of its plus end targeting. We show that the NH2-terminal microtubule-interacting domain of CLIP-170 alone localizes to microtubule plus ends when transfected into cells. Association of CLIP-...
متن کاملMicrotubule plus ends, motors, and traffic of Golgi membranes.
The intimate link between microtubule (MT) organization and the components of the secretory pathway has suggested that MT-based motility is an essential component of vesicular membrane transport and membrane polarization. The molecular details of these processes are still under investigation; however, a novel class of MT plus end-binding proteins shed new light on transport between the endoplas...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2005
ISSN: 1540-8140,0021-9525
DOI: 10.1083/jcb1721iti5