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)

Myosin-V is a versatile motor involved in short-range transport of vesicles in the actin-rich cortex of the cell. It binds to several different kinds of vesicles, and the mechanism by which it interacts with the vesicle surface is being unraveled, primarily in melanocytes. Members of the Rab family of G-proteins are required for the recruitment of myosin-V to vesicles. Rab27a and its rabphilin-like effector protein, Melanophilin, recruit myosin-Va to melanosomes and appear to serve as the membrane receptor. Myosin-V is also involved in fast axonal/dendritic transport and, interestingly, it forms a complex with kinesin, a microtubule-based motor. This kinesin/myosin-V heteromotor complex allows long-range movement of vesicles within axons and dendrites on microtubules and short-range movement in the dendritic spines and axon terminals on actin filaments. The direct interaction of motors from both filament systems may represent the mechanism by which the transition of vesicles from microtubules to actin filaments is regulated.
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PMID:Myosin-V, a versatile motor for short-range vesicle transport. 1245 49

hid-1 was originally identified as a Caenorhabditis elegans gene encoding a novel conserved protein that regulates the decision to enter into the enduring dauer larval stage. We isolated a novel allele of hid-1 in a forward genetic screen for mutants mislocalizing RBF-1 rabphilin, a RAB-27 effector. Here we demonstrate that HID-1 functions in the nervous system to regulate neuromuscular signaling and in the intestine to regulate the defecation motor program. We further show that a conserved N-terminal myristoylated motif of both invertebrate and vertebrate HID-1 is essential for its association with intracellular membranes in nematodes and PC12 cells. C. elegans neuronal HID-1 resides on intracellular membranes in neuronal cell somas; however, the kinesin UNC-104 also transports HID-1 to synaptic regions. HID-1 accumulates in the axons of unc-13 and unc-31 mutants, suggesting it is associated with neurosecretory vesicles. Consistent with this, genetic studies place HID-1 in a peptidergic signaling pathway. Finally, a hid-1 null mutation reduces the levels of endogenous neuropeptides and alters the secretion of fluorescent-tagged cargos derived from neuronal and intestinal dense core vesicles (DCVs). Taken together, our findings indicate that HID-1 is a novel component of a DCV-based neurosecretory pathway and that it regulates one or more aspects of the biogenesis, maturation, or trafficking of DCVs.
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PMID:HID-1, a new component of the peptidergic signaling pathway. 2111 72