Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.4.4 (kinesin)
 5,033 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Here we present evidence that the kinesin, Kif5B, is involved in the transportation and axonal targeting of Kv1 channels. We show that a dominant negative variant of Kif5B specifically blocks localization to the axon of expressed, tagged versions of Kv1.3 in cultured cortical slices. In addition, the dominant negative variant of Kif5B blocks axonal localization of endogenous Kv1.1, Kv1.2, and Kv1.4 in cortical neurons in dissociated cultures. We also found evidence that Kif5B interacts with Kv1 channels. Endogenous Kv1.2 colocalized with Kif5B in cortical neurons and coimmunoprecipitated with Kif5B from brain lysate. The T1 domain of Shaker K(+) channels has been shown to play a critical role in targeting the channel to the axon. We have three pieces of evidence to suggest that the T1 domain also mediates interaction between Kv1 channels and Kif5B: Addition of the T1 domain to a heterologous protein, TfR, is sufficient to cause the resulting fusion protein, TfRT1, to colocalize with Kif5B. Also, the T1 domain is necessary for interaction of Kv1.3 with Kif5B in a coimmunoprecipitation assay. Finally, dominant negative variants of Kif5B block axonal targeting of TfRT1, but have no effect on dendritic localization of TfR. Together these data suggest a model where Kif5B interacts with Kv1 channels either directly or indirectly via the T1 domain, causing the channels to be transported to axons.
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PMID:The role of Kif5B in axonal localization of Kv1 K(+) channels. 1724 Dec 75

We report on the protein-resistant properties of glass substrates coated with novel copolymers of 2-aminoethyl methacrylate hydrochloride and poly(ethylene glycol) methyl ether methacrylate (AEM-PEG). In comparison to currently available protein-blocking polymer systems, such as poly-l-lysine-poly(ethylene glycol), silane-based poly(ethylene glycol), and poly(ethylene glycol) brushes prepared by surface-initiated polymerization, the proposed AEM-PEG offers the combined advantages of low cost, simplicity of use, and applicability in aqueous solutions. We demonstrate the capability of AEM-PEG to block the surface binding of globular proteins (tubulin), their assemblies (microtubules), and functional motor proteins (kinesin-1). Moreover, we demonstrate the applicability of AEM-PEG for surface patterning of proteins in microfluidic devices.
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PMID:Protein-resistant polymer coatings based on surface-adsorbed poly(aminoethyl methacrylate)/poly(ethylene glycol) copolymers. 2000 Apr 61