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Cargo of Kinesin Identified as Jip Scaffolding Proteins and Associated Signaling Molecules
Results demonstrate a direct interaction between conventional kinesin and a cargo, indicate that motor proteins are linked to their membranous cargo via scaffolding proteins, and support a role for motor proteins in spatial regulation of signal transduction pathways. Expand
Microtubule Acetylation Promotes Kinesin-1 Binding and Transport
It is shown that the kinesin-1 cargo protein JNK-interacting protein 1 (JIP1) is localized to only a subset of neurites in cultured neuronal cells, and microtubule PTMs are important markers of distinct microtubules populations and that they act to control motor-protein trafficking. Expand
Traffic control: regulation of kinesin motors
This work has revealed molecular mechanisms that control kinesin autoinhibition and subsequent activation, binding to cargos and microtubule tracks, and localization at specific sites of action. Expand
A Size-Exclusion Permeability Barrier and Nucleoporins Characterize a Ciliary Pore Complex that Regulates Transport into Cilia
It is demonstrated that nucleoporins localize to the base of primary and motile cilia and that microinjection ofucleoporin-function-blocking reagents blocks the ciliary entry of kinesin-2 KIF17 motors. Expand
ER sliding dynamics and ER–mitochondrial contacts occur on acetylated microtubules
Movement of the ER and mitochondria is coupled by limited interactions of the ER with a subset of posttranslationally modified microtubules.
Tubulin modifications and their cellular functions.
Recent studies demonstrating that tubulin modifications influence microtubule-associated proteins such as severing proteins, plus-end tracking proteins, and molecular motors play an important role in regulatingmicrotubule properties, such as stability and structure, as well as microtubules-based functions, suchAs ciliary beating, cell division, and intracellular trafficking. Expand
Two binding partners cooperate to activate the molecular motor Kinesin-1
It is shown that binding of JIP1 and FEZ1 to Kinesin-1 is sufficient to activate the motor for MT binding and motility, the first demonstration of the activation of a MT-based motor by cellular binding partners. Expand
Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules
Evidence is provided that a function of LC is to keep kinesin in an inactive ground state by inducing an interaction between the tail and motor domains of HC; activation for cargo transport may be triggered by a small conformational change that releases the inhibition of the motor domain for MT binding. Expand
Ciliary Targeting of Olfactory CNG Channels Requires the CNGB1b Subunit and the Kinesin-2 Motor Protein, KIF17
It is shown that heteromeric assembly with CNGB1b, containing a critical carboxy-terminal motif (RVxP), is required for ciliary trafficking of olfactory CNG channels. Expand
Single Molecule Imaging Reveals Differences in Microtubule Track Selection Between Kinesin Motors
Molecular motors differentially recognize and move cargo along discrete microtubule subpopulations in cells, resulting in preferential transport and targeting of subcellular cargoes.