Identification of the human homologue of mouse KIF4, a kinesin superfamily motor protein

Oh, Seong-Hwan; Hahn, Hwa-Sun; Torrey, Ted A.; Shin, Hyunjin; Choi, Won‐Young; Lee, Young Mi; Morse, Herbert C.; Kim, Wankee

doi:10.1016/s0167-4781(00)00151-2

Cited by 14 publications

(15 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In terms of sequence similarity and subcellular distribution, human KIF4 is most closely related to murine KIF4, and it has been suggested that human KIF4 possesses similar functions to those of murine KIF4. However, in spite of 68 % amino acid similarity between them, the presence of several divergent regions in the binding domain [20] underscores the possibility that human KIF4 is not a functional orthologue of murine KIF4. As an initial step to address the function of human KIF4, we examined its localization and chromosomal association in the present study.…”

Section: Discussionmentioning

confidence: 99%

“…H, human (Homo sapiens) [20] ; M, mouse (Mus musculus) [17] ; C, chick (Gallus gallus) [24]; F, frog (Xenopus laevis) [25].…”

Section: Table 1 Sequence Comparison Of Four Nls Candidates In Kif4 Mmentioning

confidence: 99%

“…Of these, murine KIF4 was isolated from mouse brains and was found to be an anterograde motor protein for transporting membranous organelles in juvenile neurons and other cells [16,17]. Recent studies [18,19] showing that murine KIF4 proteins were possibly associated with those of various retroviruses, including HIV type 1, led to the identification of a human counterpart of murine KIF4 [20]. Human KIF4 cDNA consists of a 60 bp 5h untranslated region (UTR), a 3696 bp open reading frame (ORF) and a 740 bp complete 3h UTR, and is predicted to encode a 140 kDa protein of 1232 amino acids.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Human kinesin superfamily member 4 is dominantly localized in the nuclear matrix and is associated with chromosomes during mitosis

LEE

et al. 2001

Biochemical Journal

Self Cite

View full text Add to dashboard Cite

In a previous study, we identified the human counterpart of murine kinesin superfamily member 4 (KIF4), a microtubule-based motor protein [Oh, Hahn, Torrey, Shin, Choi, Lee, Morse and Kim (2000) Biochim. Biophys. Acta 1493, 219–224]. As an initial step to understand the function(s) of human KIF4, its subcellular localization in HeLa cells was examined by using immunocytochemical and subcellular fractionation methods, and it was found that most KIF4 is localized in the nucleus. Since murine KIF4 is known to transport cytoplasmic vesicles, dominant nuclear localization of the human counterpart was somewhat surprising. Subsequent subnuclear fractionation revealed predominant association of KIF4 with the nuclear matrix. These results clearly indicate that human KIF4 is, at least, a nuclear protein. In further confirmation of this conclusion, the hexapeptide PKLRRR (amino acids 773–778) in the molecule was found to function as a nuclear localization signal. During the mitotic phase of the cell cycle, human KIF4 was associated with the chromosomes, suggesting that human KIF4 might be a microtubule-based mitotic motor, with DNA as its cargo.

show abstract

Section: Discussionmentioning

confidence: 99%

“…H, human (Homo sapiens) [20] ; M, mouse (Mus musculus) [17] ; C, chick (Gallus gallus) [24]; F, frog (Xenopus laevis) [25].…”

Section: Table 1 Sequence Comparison Of Four Nls Candidates In Kif4 Mmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Human kinesin superfamily member 4 is dominantly localized in the nuclear matrix and is associated with chromosomes during mitosis

LEE

et al. 2001

Biochemical Journal

Self Cite

View full text Add to dashboard Cite

show abstract

“…Like KIF4 proteins, FRA1 has an N-terminal motor domain that presumably is involved in binding to and movement along microtubules in the expense of ATP hydrolysis and a C-terminal tail region, which are separated by a long coiled-coil region ( Figure 7C). The FRA1 motor domain (amino acid residues 1 to 384) shares 51% amino acid sequence identity and 63% similarity with the motor domains of human KIF4 ( Figure 7B) (Oh et al, 2000). It contains all of the conserved motifs present in the motor domains of typical kinesins.…”

Section: Sequence Analysis Of the Fra1 Proteinmentioning

confidence: 99%

A Kinesin-Like Protein Is Essential for Oriented Deposition of Cellulose Microfibrils and Cell Wall Strength

et al. 2002

View full text Add to dashboard Cite

Cortical microtubules have long been hypothesized to regulate the oriented deposition of cellulose microfibrils. However, the molecular mechanisms of how microtubules direct the orientation of cellulose microfibril deposition are not known. We have used fibers in the inflorescence stems of Arabidopsis to study secondary wall deposition and cell wall strength and found a fragile fiber ( fra1 ) mutant with a dramatic reduction in the mechanical strength of fibers. The fra1 mutation did not cause any defects in cell wall composition, secondary wall thickening, or cortical microtubule organization in fiber cells. An apparent alteration was found in the orientation of cellulose microfibrils in fra1 fiber walls, indicating that the reduced mechanical strength of fra1 fibers probably was attributable to altered cellulose microfibril deposition. The FRA1 gene was cloned and found to encode a kinesin-like protein with an N-terminal microtubule binding motor domain. The FRA1 protein was shown to be concentrated around the periphery of the cytoplasm but absent in the nucleus. Based on these findings, we propose that the FRA1 kinesin-like protein is involved in the microtubule control of cellulose microfibril order.

show abstract

“…KIF4A (hereby denoted KIF4) is a plus-end-directed, microtubule (MT)-stimulated ATPase in the kinesin motor family (24,34). KIF4 contains a characteristic N-terminal motor domain, which binds MTs and ATP and is responsible for force generation along MTs (10,16,45).…”

mentioning

confidence: 99%

Kinesin KIF4 Regulates Intracellular Trafficking and Stability of the Human Immunodeficiency Virus Type 1 Gag Polyprotein

Martinez

Xue²,

Berro

et al. 2008

J Virol

View full text Add to dashboard Cite

Retroviral Gag proteins are synthesized as soluble, myristoylated precursors that traffic to the plasma membrane and promote viral particle production. The intracellular transport of human immunodeficiency virus type 1 (HIV-1) Gag to the plasma membrane remains poorly understood, and cellular motor proteins responsible for Gag movement are not known. Here we show that disrupting the function of KIF4, a kinesin family member, slowed temporal progression of Gag through its trafficking intermediates and inhibited virus-like particle production. Knockdown of KIF4 also led to increased Gag degradation, resulting in reduced intracellular Gag protein levels; this phenotype was rescued by reintroduction of KIF4. When KIF4 function was blocked, Gag transiently accumulated in discrete, perinuclear, nonendocytic clusters that colocalized with endogenous KIF4, with Ubc9, an E2 SUMO-1 conjugating enzyme, and with SUMO. These studies identify a novel transit station through which Gag traffics en route to particle assembly and highlight the importance of KIF4 in regulating HIV-1 Gag trafficking and stability.

show abstract

Identification of the human homologue of mouse KIF4, a kinesin superfamily motor protein

Cited by 14 publications

References 20 publications

Human kinesin superfamily member 4 is dominantly localized in the nuclear matrix and is associated with chromosomes during mitosis

Human kinesin superfamily member 4 is dominantly localized in the nuclear matrix and is associated with chromosomes during mitosis

A Kinesin-Like Protein Is Essential for Oriented Deposition of Cellulose Microfibrils and Cell Wall Strength

Kinesin KIF4 Regulates Intracellular Trafficking and Stability of the Human Immunodeficiency Virus Type 1 Gag Polyprotein

Contact Info

Product

Resources

About