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)

Vigorous investigation has finally begun to shed light on the cargo problem of the microtubule-dependent motors, kinesin and dynein superfamily proteins. Biochemical observations have suggested that the potential cargoes of certain populations of motor proteins seem to be in vesicle-form, each vesicle possessing specific functional marker molecules. In addition to the close relationship between microtubule-dependent motors and cargoes in vesicle-form, kinesin has also been highlighted as an apparent driving force for another cargo in non-vesicle-form, cytoplasmic protein. On the basis of new biophysical and cell-biological evidence, the controversy over the movement of cytoplasmic cargoes has entered a new phase.
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PMID:Moving on to the cargo problem of microtubule-dependent motors in neurons. 1108 18

Fertilization in Chlamydomonas begins with flagellar adhesion between mating type plus and mating type minus gametes and is consummated within minutes by zygote formation. Once fusion occurs, the newly merged gametes cease existence as distinct entities, and the diploid zygote immediately initiates transcription of zygote-specific genes. Accomplishing fertilization within such a short time requires the rapid and signaled movement of pre-existing membrane and cytoplasmic proteins between and within several cellular compartments. Generation within the adhering flagella of the initial signals for protein movement, as well as movement itself of at least one cytoplasmic protein from the cell body to the flagella, depend on the microtubule motor, kinesin-II and presumably on intraflagellar transport (IFT). Adhesion and fusion of the two gametes depend on a second translocation event, the movement of an adhesion/fusion protein onto the surface of a rapidly elongating, microvillous-like fusion organelle. Finally, the merging of the two separate gametes, each containing sex-specific proteins, into a single cell allows the formerly separate proteins to form new interactions that regulate zygote development. Two proteins - a nuclease and a homeodomain protein - which were present only in the plus gamete, are 'delivered' to the cytoplasm of the zygote during gamete fusion. The nuclease is selectively imported into the minus chloroplast, where it degrades the chloroplast DNA, thereby ensuring uniparental inheritance of plus chloroplast traits. The homeodomain protein binds with an as yet unidentified protein delivered by the minus gamete, and the new complex activates transcription of zygote-specific genes.
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PMID:Protein transport and signal transduction during fertilization in chlamydomonas. 1279 90

Mitochondrial fusion in plants and its role in development are poorly understood. Cultured tobacco mesophyll protoplasts provide an excellent experimental system for visualizing mitochondrial dynamics. Before protoplasts first divide, mitochondria undergo a phase of extensive elongation before fission causes an increase in number, followed by actin filament (AF)-dependent dispersion that distributes mitochondria uniformly throughout the cytoplasm. Here, by fusing protoplasts containing either green fluorescent protein- or MitoTracker-labelled mitochondria, we show that elongation results from fusion during early (4-8 h) protoplast culture. This massive mitochondrial fusion (MMF) leads to near-complete mixing of the mitochondrial population within 24 h. Staining isolated mitochondria with 4',6-diamidino-2-phenylindole (DAPI) revealed that in freshly prepared protoplasts mitochondrial nucleoids were unequally distributed, with many mitochondria failing to stain with DAPI, suggesting the presence of an incomplete mitochondrial genome. Following MMF, nucleoids were distributed evenly throughout the population, thereby ensuring continuity of the mitochondrial genome in daughter cells. Massive mitochondrial fusion appears to be specific to dedifferentiation, since it also occurs in mesophyll protoplasts of Arabidopsis and Medicago but not in protoplasts from already dedifferentiated cells such as BY-2 or callus cultures. Efficient MMF requires an inner membrane electrical gradient, cytoplasmic protein synthesis, microtubules and functional kinesin but not ATP or AFs, indicating fundamental differences from mitochondrial fusion in non-plant systems. Our studies reveal that individual mitochondria are connected over time by fusion events, a finding that allows a clearer interpretation of how novel mitochondrial genotypes develop following cell fusion, and indicates that developmentally regulated fusion ensures continuity of the mitochondrial genome.
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PMID:Mitochondria as a connected population: ensuring continuity of the mitochondrial genome during plant cell dedifferentiation through massive mitochondrial fusion. 1629 67

Site-specific fluorescent labeling of proteins inside live mammalian cells has been achieved by employing Streptolysin O, a bacterial enzyme which forms temporary pores in the membrane and allows delivery of virtually any fluorescent probes, ranging from labeled IgG's to small ligands, with high efficiency (>85% of cells). The whole process, including recovery, takes 30 min, and the cell is ready to be imaged immediately. A variety of cell viability tests were performed after treatment with SLO to ensure that the cells have intact membranes, are able to divide, respond normally to signaling molecules, and maintains healthy organelle morphology. When combined with Oxyrase, a cell-friendly photostabilizer, a ~20x improvement in fluorescence photostability is achieved. By adding in glutathione, fluorophores are made to blink, enabling super-resolution fluorescence with 20-30 nm resolution over a long time (~30 min) under continuous illumination. Example applications in conventional and super-resolution imaging of native and transfected cells include p65 signal transduction activation, single molecule tracking of kinesin, and specific labeling of a series of nuclear and cytoplasmic protein complexes.
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PMID:Labeling proteins inside living cells using external fluorophores for microscopy. 2814 24