All kinesin superfamily protein, KIF, genes in mouse and human

Miki, Hiromi; Setou, Mitsutoshi; Kaneshiro, Kiyofumi; Hirokawa, Nobutaka

doi:10.1073/pnas.111145398

Cited by 594 publications

(483 citation statements)

References 125 publications

Supporting

Mentioning

475

Contrasting

Unclassified

Order By: Relevance

“…CENP-F (mitosin) associates with the centromere-kinetochore complex from the onset of mitosis to the metaphase (Rattner et al, 1993), gradually accumulates during the cell cycle and peaks in G 2 and M phase cells, and is then rapidly degraded upon the completion of mitosis (Liao et al, 1995). KIF4A belongs to the kinesinlike protein family, and is fundamental to many biological processes, including cell division, and the intracellular transport of membranous organelles in higher eukaryotic cells (Miki et al, 2001). KIF4A might play an important role in mitotic chromosomal positioning and bipolar spindle stabilization .…”

Section: Discussionmentioning

confidence: 99%

Exploration of replicative senescence-associated genes in human dermal fibroblasts by cDNA microarray technology

Yoon

Kim

et al. 2004

Experimental Gerontology

109

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

Exploration of replicative senescence-associated genes in human dermal fibroblasts by cDNA microarray technology

Yoon

Kim

et al. 2004

Experimental Gerontology

109

View full text Add to dashboard Cite

“…Kinesins are classified according to the position of the highly conserved motor domain (binds MTs) which may be N-terminal (N-kinesin), middle (M-kinesin) or C-terminal (Ckinesin) [75,77,78]. The majority of kinesins are Nkinesins which transport cargo such as membranous vesicles, protein complexes, mRNA and viruses towards the plus or growing end of MTs [73][74][75].…”

Section: Kinesinmentioning

confidence: 99%

Transport and egress of herpes simplex virus in neurons

Diefenbach

Miranda-Saksena

Douglas

et al. 2007

Reviews in Medical Virology

171

150

View full text Add to dashboard Cite

The mechanisms of axonal transport of the alphaherpesviruses, HSV and pseudorabies virus (PrV), in neuronal axons are of fundamental interest, particularly in comparison with other viruses, and offer potential sites for antiviral intervention or development of gene therapy vectors. These herpesviruses are transported rapidly along microtubules (MTs) in the retrograde direction from the axon terminus to the dorsal root ganglion and then anterogradely in the opposite direction. Retrograde transport follows fusion and deenvelopment of the viral capsid at the axonal membrane followed by loss of most of the tegument proteins and then binding of the capsid via one or more viral proteins (VPs) to the retrograde molecular motor dynein. The HSV capsid protein pUL35 has been shown to bind to the dynein light chain Tctex1 but is likely to be accompanied by additional dynein binding of an inner tegument protein. The mechanism of anterograde transport is much more controversial with different processes being claimed for PrV and HSV: separate transport of HSV capsid/tegument and glycoproteins versus PrV transport as an enveloped virion. The controversy has not been resolved despite application, in several laboratories, of confocal microscopy (CFM), realtime fluorescence with viruses dual labelled on capsid and glycoprotein, electron microscopy in situ and immunoelectron microscopy. Different processes for each virus seem counterintuitive although they are the most divergent in the alphaherpesvirus subfamily. Current hypotheses suggest that unenveloped HSV capsids complete assembly in the axonal growth cones and varicosities, whereas with PrV unenveloped capsids are only found travelling in a retrograde direction.

show abstract

“…However, CHO1 represents a unique isotype, in which an actin-binding sequence encoded by exon 18 is included in the middle of the tail domain . Members of the MKLP1 subfamily (Miki et al, 2001) have been shown to function in cytokinesis in different species (Adams et al, 1998;Powers et al, 1998;Raich et al, 1998;Chen et al, 2002;Matuliene and Kuriyama, 2002). In humans and C. elegans, the motor proteins interact with a GAP for Rho family GTPases, which facilitates microtubule bundling and formation of the spindle midzone and midbody (Mishima et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Role of the Midbody Matrix in Cytokinesis: RNAi and Genetic Rescue Analysis of the Mammalian Motor Protein CHO1

Matulienė

Kuriyama

2004

MBoC

View full text Add to dashboard Cite

CHO1 is a kinesin-like motor protein essential for cytokinesis in mammalian cells. To analyze how CHO1 functions, we established RNAi and genetic rescue assays. CHO1-depleted cells reached a late stage of cytokinesis but fused back to form binucleate cells because of the absence of the midbody matrix in the middle of the intercellular bridge. Expression of exogenous CHO1 restored the formation of the midbody matrix and rescued cytokinesis in siRNA-treated cells. By analyzing phenotypes rescued with different constructs, it was shown that both motor and stalk domains function in midbody formation, whereas the tail is essential for completion of cytokinesis after the midbody matrix has formed. During the terminal stage of cytokinesis, different subregions of the tail play distinctive roles in stabilizing the midbody matrix and maintaining an association between the midbody and cell cortex. These results demonstrate that CHO1 consists of functionally differentiated subregions that act in concert to ensure complete cell separation.

show abstract

All kinesin superfamily protein, KIF, genes in mouse and human

Cited by 594 publications

References 125 publications

Exploration of replicative senescence-associated genes in human dermal fibroblasts by cDNA microarray technology

Exploration of replicative senescence-associated genes in human dermal fibroblasts by cDNA microarray technology

Transport and egress of herpes simplex virus in neurons

Role of the Midbody Matrix in Cytokinesis: RNAi and Genetic Rescue Analysis of the Mammalian Motor Protein CHO1

Contact Info

Product

Resources

About