KIF3B

Last updated
KIF3B
KIF3B.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases KIF3B , FLA8, HH0048, KLP-11, kinesin family member 3B, RP89
External IDs OMIM: 603754 MGI: 107688 HomoloGene: 55849 GeneCards: KIF3B
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004798

NM_008444

RefSeq (protein)

NP_004789

NP_032470

Location (UCSC) Chr 20: 32.28 – 32.34 Mb Chr 2: 153.13 – 153.18 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Kinesin-like protein KIF3B is a protein that in humans is encoded by the KIF3B gene. [5] [6] KIF3B is an N-type protein that complexes with two other kinesin proteins to form two-headed anterograde motors. [7] First, KIF3B forms a heterodimer with KIF3A (kinesin-like protein KIF3A); (KIF3A/3B), that is membrane-bound and has ATPase activity. Then KIFAP3 (KAP3, kinesin superfamily associated protein–3) binds to the tail domain to form a heterotrimeric motor. [7] This motor has a plus end-directed microtubule sliding activity that exhibits a velocity of ~0.3 μm/s a. [8] There are 14 kinesin protein families in the kinesin superfamily and KIF3B is part of the Kinesin-2 family, of kinesins that can all form heterotrimeric complexes. [9] Expression of the three motor subunits is ubiquitous. The KIG3A/3B/KAP3 motors can transport 90 to 160 nm in diameter organelles. [7]

Contents

There are many orthologous KIF3B genes that are expressed in Drosophila , the sea urchin, Bos taurus , Canis familiaris , Equus caballus , Felis catus , Macaca mulatta , Mus musculus , Pan troglodytes , and Rattus norvegicus .

Function

The heterotrimeric KIF3B/KIF3A/KAP3 motor machinery functions in the intracellular transport of multiple different molecules such as β-catenin and MT1-MMP. [10] [11] KIF3B activity has been implicated with various cellular processes such as intracellular movement of organelles, intraflagellar transport, chromosome movement during mitosis and meiosis, and cellular interaction with the extracellular matrix. [6] [12] [13]

KIF3B also regulates the interaction of cancer cells with the extracellular matrix (ECM), in particular the transport of MT1-MMP to the cancer cell front is essential for collagen fiber matrix realignment and degradation. [14] [15]

Interactions

KIF3B has been shown to interact with the SMC3 subunit of the cohesin complex and with RAB4A. [16]

Related Research Articles

<span class="mw-page-title-main">Microtubule</span> Polymer of tubulin that forms part of the cytoskeleton

Microtubules are polymers of tubulin that form part of the cytoskeleton and provide structure and shape to eukaryotic cells. Microtubules can be as long as 50 micrometres, as wide as 23 to 27 nm and have an inner diameter between 11 and 15 nm. They are formed by the polymerization of a dimer of two globular proteins, alpha and beta tubulin into protofilaments that can then associate laterally to form a hollow tube, the microtubule. The most common form of a microtubule consists of 13 protofilaments in the tubular arrangement.

<span class="mw-page-title-main">Spindle apparatus</span> Feature of biological cell structure

In cell biology, the spindle apparatus is the cytoskeletal structure of eukaryotic cells that forms during cell division to separate sister chromatids between daughter cells. It is referred to as the mitotic spindle during mitosis, a process that produces genetically identical daughter cells, or the meiotic spindle during meiosis, a process that produces gametes with half the number of chromosomes of the parent cell.

<span class="mw-page-title-main">Kinesin</span> Eukaryotic motor protein

A kinesin is a protein belonging to a class of motor proteins found in eukaryotic cells. Kinesins move along microtubule (MT) filaments and are powered by the hydrolysis of adenosine triphosphate (ATP). The active movement of kinesins supports several cellular functions including mitosis, meiosis and transport of cellular cargo, such as in axonal transport, and intraflagellar transport. Most kinesins walk towards the plus end of a microtubule, which, in most cells, entails transporting cargo such as protein and membrane components from the center of the cell towards the periphery. This form of transport is known as anterograde transport. In contrast, dyneins are motor proteins that move toward the minus end of a microtubule in retrograde transport.

<span class="mw-page-title-main">Dynein</span> Class of enzymes

Dyneins are a family of cytoskeletal motor proteins that move along microtubules in cells. They convert the chemical energy stored in ATP to mechanical work. Dynein transports various cellular cargos, provides forces and displacements important in mitosis, and drives the beat of eukaryotic cilia and flagella. All of these functions rely on dynein's ability to move towards the minus-end of the microtubules, known as retrograde transport; thus, they are called "minus-end directed motors". In contrast, most kinesin motor proteins move toward the microtubules' plus-end, in what is called anterograde transport.

<span class="mw-page-title-main">Motor protein</span> Class of molecular proteins

Motor proteins are a class of molecular motors that can move along the cytoplasm of cells. They convert chemical energy into mechanical work by the hydrolysis of ATP. Flagellar rotation, however, is powered by a proton pump.

<span class="mw-page-title-main">Dynactin</span>

Dynactin is a 23 subunit protein complex that acts as a co-factor for the microtubule motor cytoplasmic dynein-1. It is built around a short filament of actin related protein-1 (Arp1).

<span class="mw-page-title-main">KIF23</span> Protein-coding gene in the species Homo sapiens

Kinesin-like protein KIF23 is a protein that in humans is encoded by the KIF23 gene.

<span class="mw-page-title-main">KIF5B</span> Protein-coding gene in the species Homo sapiens

Kinesin family member 5B (KIF5B) is a protein that in humans is encoded by the KIF5B gene. It is part of the kinesin family of motor proteins.

<span class="mw-page-title-main">KIF4A</span> Protein-coding gene in the species Homo sapiens

Kinesin family member 4A is a protein that in humans is encoded by the KIF4A gene.

<span class="mw-page-title-main">KIF2C</span> Protein-coding gene in the species Homo sapiens

Kinesin-like protein KIF2C is a protein that in humans is encoded by the KIF2C gene.

<span class="mw-page-title-main">KIF3A</span> Protein-coding gene in the species Homo sapiens

Kinesin-like protein KIF3A is a protein that in humans is encoded by the KIF3A gene.

<span class="mw-page-title-main">KIF20A</span> Protein-coding gene in the species Homo sapiens

Kinesin-like protein KIF20A is a protein that in humans is encoded by the KIF20A gene.

<span class="mw-page-title-main">Kinesin-associated protein 3</span> Protein-coding gene in the species Homo sapiens

Kinesin-associated protein 3 (KAP3) is a protein that in humans is encoded by the KIFAP3 gene. It is a non-motor, accessory subunit which co-oligomerizes with the motor subunits KIF3A and KIF3B or KIF3C, to form heterotrimeric kinesin-2 motor proteins. Kinesin-2 KAP subunits were initially characterized in echinoderms and mice.

<span class="mw-page-title-main">KIF5A</span> Protein-coding gene in humans

Kinesin family member 5A is a protein that in humans is encoded by the KIF5A gene. It is part of the kinesin family of motor proteins.

<span class="mw-page-title-main">KIFC1</span> Protein-coding gene in the species Homo sapiens

Kinesin-like protein KIFC1 is a protein that in humans is encoded by the KIFC1 gene.

<span class="mw-page-title-main">KIF17</span> Protein-coding gene in the species Homo sapiens

Kinesin-like protein KIF17 is a protein that in humans is encoded by the KIF17 gene. KIF17 and its close relative, C. elegans OSM-3, are members of the kinesin-2 family of plus-end directed microtubule-based motor proteins. In contrast to heterotrimeric kinesin-2 motors, however, KIF17 and OSM-3 form distinct homodimeric complexes. Homodimeric kinesin-2 has been implicated in the transport of NMDA receptors along dendrites for delivery to the dendritic membrane, whereas both heterotrimeric and homodimeric kinesin-2 motors function cooperatively in anterograde intraflagellar transport (IFT) and cilium biogenesis.

<span class="mw-page-title-main">KIF1A</span> Motor protein in humans

Kinesin-like protein KIF1A, also known as axonal transporter of synaptic vesicles or microtubule-based motor KIF1A, is a protein that in humans is encoded by the KIF1A gene.

<span class="mw-page-title-main">Kinesin-like protein KIF11</span> Protein-coding gene in the species Homo sapiens

Kinesin-like protein KIF11 is a molecular motor protein that is essential in mitosis. In humans it is coded for by the gene KIF11. Kinesin-like protein KIF11 is a member of the kinesin superfamily, which are nanomotors that move along microtubule tracks in the cell. Named from studies in the early days of discovery, it is also known as Kinesin-5, or as BimC, Eg5 or N-2, based on the founding members of this kinesin family.

<span class="mw-page-title-main">KIF15</span> Protein-coding gene in the species Homo sapiens

Kinesin family member 15 is a protein that in humans is encoded by the KIF15 gene.

Nobutaka Hirokawa is a Japanese neuroscientist and cell biologist famous for research on the kinesin superfamily of motor proteins. He has been President and Chair of the Board of Trustees at the Human Frontier Science Program since 2012.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000101350 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027475 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, et al. (April 1997). "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Research. 4 (2): 141–50. doi: 10.1093/dnares/4.2.141 . PMID   9205841.
  6. 1 2 "Entrez Gene: KIF3B kinesin family member 3B".
  7. 1 2 3 Hirokawa N (January 1998). "Kinesin and dynein superfamily proteins and the mechanism of organelle transport". Science. 279 (5350): 519–26. Bibcode:1998Sci...279..519H. doi:10.1126/science.279.5350.519. PMID   9438838.
  8. Hirokawa N (January 1998). "Kinesin and dynein superfamily proteins and the mechanism of organelle transport". Science. 279 (5350): 519–26. Bibcode:1998Sci...279..519H. doi:10.1126/science.279.5350.519. PMID   9438838.
  9. Lawrence CJ, Dawe RK, Christie KR, Cleveland DW, Dawson SC, Endow SA, et al. (October 2004). "A standardized kinesin nomenclature". The Journal of Cell Biology. 167 (1): 19–22. doi:10.1083/jcb.200408113. PMC   2041940 . PMID   15479732.
  10. Jimbo T, Kawasaki Y, Koyama R, Sato R, Takada S, Haraguchi K, Akiyama T (April 2002). "Identification of a link between the tumour suppressor APC and the kinesin superfamily". Nature Cell Biology. 4 (4): 323–7. doi:10.1038/ncb779. PMID   11912492. S2CID   10745049.
  11. Wiesner C, Faix J, Himmel M, Bentzien F, Linder S (September 2010). "KIF5B and KIF3A/KIF3B kinesins drive MT1-MMP surface exposure, CD44 shedding, and extracellular matrix degradation in primary macrophages". Blood. 116 (9): 1559–69. doi: 10.1182/blood-2009-12-257089 . PMID   20505159.
  12. Scholey JM (April 1996). "Kinesin-II, a membrane traffic motor in axons, axonemes, and spindles". The Journal of Cell Biology. 133 (1): 1–4. doi:10.1083/jcb.133.1.1. PMC   2120781 . PMID   8601599.
  13. Lawrence CJ, Dawe RK, Christie KR, Cleveland DW, Dawson SC, Endow SA, et al. (October 2004). "A standardized kinesin nomenclature". The Journal of Cell Biology. 167 (1): 19–22. doi:10.1083/jcb.200408113. PMC   2041940 . PMID   15479732.
  14. Kravtsov O, Hartley CP, Compérat EM, Iczkowski KA (2019). "KIF3B protein expression loss correlates with metastatic ability of prostate cancer". American Journal of Clinical and Experimental Urology. 7 (3): 178–181. PMC   6627541 . PMID   31317057.
  15. Stoletov K, Willetts L, Paproski RJ, Bond DJ, Raha S, Jovel J, et al. (June 2018). "Quantitative in vivo whole genome motility screen reveals novel therapeutic targets to block cancer metastasis". Nature Communications. 9 (1): 2343. Bibcode:2018NatCo...9.2343S. doi: 10.1038/s41467-018-04743-2 . PMC   6002534 . PMID   29904055.
  16. Imamura T, Huang J, Usui I, Satoh H, Bever J, Olefsky JM (July 2003). "Insulin-induced GLUT4 translocation involves protein kinase C-lambda-mediated functional coupling between Rab4 and the motor protein kinesin". Molecular and Cellular Biology. 23 (14): 4892–900. doi:10.1128/MCB.23.14.4892-4900.2003. PMC   162221 . PMID   12832475.

Further reading