Health Dictionary
Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
KIF3B
Introduction
Kinesin-like protein KIF3B is a protein that in humans is encoded by the KIF3B gene.[1][2]
Function
Function
The protein encoded by this gene forms a heterotrimeric motor complex with kinesin family member 3A and KAP3 (kinesin accessory protein 3) to drive intra-flagellar transport and possibly to aid in chromosome movement during mitosis and meiosis. The encoded protein is a plus end-directed microtubule motor and can interact with the SMC3 subunit of the cohesin complex. In addition, the encoded protein may be involved in the intracellular movement of membranous organelles. The heterotrimeric KIF3B/KIF3A/KAP3 motor protein is a member of the kinesin-2 subfamily of the kinesin superfamily.[2][3][4]
Model organisms
Model organisms
Model organisms have been used in the study of KIF3B function. A conditional knockout mouse line called Kif3btm1b(EUCOMM)Wtsi was generated at the Wellcome Trust Sanger Institute.[6] Male and female animals underwent a standardized phenotypic screen[7] to determine the effects of deletion.[8][9][10][11] Additional screens performed: – In-depth immunological phenotyping[12]
| Characteristic | Phenotype |
|---|---|
| All data available at.[7][12] | |
| Peripheral blood leukocytes 6 Weeks | Abnormal |
| Insulin | Normal |
| Haematology 6 Weeks | Normal |
| Homozygous viability at P14 | Abnormal |
| Recessive lethal study | Abnormal |
| Body weight | Normal |
| Neurological assessment | Normal |
| Grip strength | Normal |
| Dysmorphology | Normal |
| Indirect calorimetry | Normal |
| Glucose tolerance test | Normal |
| Auditory brainstem response | Normal |
| DEXA | Normal |
| Radiography | Normal |
| Eye morphology | Normal |
| Clinical chemistry | Normal |
| Haematology 16 Weeks | Normal |
| Peripheral blood leukocytes 16 Weeks | Normal |
| Heart weight | Normal |
| Salmonella infection | Normal |
| Cytotoxic T Cell Function | Normal |
| Spleen Immunophenotyping | Normal |
| Mesenteric Lymph Node Immunophenotyping | Normal |
| Bone Marrow Immunophenotyping | Normal |
| Epidermal Immune Composition | Normal |
References
References
- ↑ Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Apr 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.
- ↑ 2.0 2.1 “Entrez Gene: KIF3B kinesin family member 3B”.
- ↑ Scholey JM (Apr 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.
- ↑ Lawrence CJ, Dawe RK, Christie KR, Cleveland DW, Dawson SC, Endow SA, Goldstein LS, Goodson HV, Hirokawa N, Howard J, Malmberg RL, McIntosh JR, Miki H, Mitchison TJ, Okada Y, Reddy AS, Saxton WM, Schliwa M, Scholey JM, Vale RD, Walczak CE, Wordeman L (Oct 2004). “A standardized kinesin nomenclature”. The Journal of Cell Biology. 167 (1): 19–22. doi:10.1083/jcb.200408113. PMC 2041940. PMID 15479732.
- ↑ Imamura T, Huang J, Usui I, Satoh H, Bever J, Olefsky JM (Jul 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.
- ↑ Gerdin AK (2010). “The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice”. Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
- ↑ 7.0 7.1 “International Mouse Phenotyping Consortium”.
- ↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). “A conditional knockout resource for the genome-wide study of mouse gene function”. Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
- ↑ Dolgin E (Jun 2011). “Mouse library set to be knockout”. Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
- ↑ Collins FS, Rossant J, Wurst W (Jan 2007). “A mouse for all reasons”. Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
- ↑ White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). “Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes”. Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
- ↑ 12.0 12.1 “Infection and Immunity Immunophenotyping (3i) Consortium”.
Further reading
Further reading
- Yamazaki H, Nakata T, Okada Y, Hirokawa N (Sep 1995). “KIF3A/B: a heterodimeric kinesin superfamily protein that works as a microtubule plus end-directed motor for membrane organelle transport”. The Journal of Cell Biology. 130 (6): 1387–99. doi:10.1083/jcb.130.6.1387. PMC 2120571. PMID 7559760.
- Nagata KI, Puls A, Futter C, Aspenstrom P, Schaefer E, Nakata T, Hirokawa N, Hall A (Jan 1998). “The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3”. The EMBO Journal. 17 (1): 149–58. doi:10.1093/emboj/17.1.149. PMC 1170366. PMID 9427749.
- Shimizu K, Shirataki H, Honda T, Minami S, Takai Y (Mar 1998). “Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated protein, with a human chromosome-associated polypeptide”. The Journal of Biological Chemistry. 273 (12): 6591–4. doi:10.1074/jbc.273.12.6591. PMID 9506951.
- Nonaka S, Tanaka Y, Okada Y, Takeda S, Harada A, Kanai Y, Kido M, Hirokawa N (Dec 1998). “Randomization of left-right asymmetry due to loss of nodal cilia generating leftward flow of extraembryonic fluid in mice lacking KIF3B motor protein”. Cell. 95 (6): 829–37. doi:10.1016/S0092-8674(00)81705-5. PMID 9865700.
- Navarro E, Espinosa L, Adell T, Torà M, Berrozpe G, Real FX (Jul 1999). “Expressed sequence tag (EST) phenotyping of HT-29 cells: cloning of ser/thr protein kinase EMK1, kinesin KIF3B, and of transcripts that include Alu repeated elements”. Biochimica et Biophysica Acta. 1450 (3): 254–64. doi:10.1016/S0167-4889(99)00051-8. PMID 10395937.
- Whitehead JL, Wang SY, Bost-Usinger L, Hoang E, Frazer KA, Burnside B (Nov 1999). “Photoreceptor localization of the KIF3A and KIF3B subunits of the heterotrimeric microtubule motor kinesin II in vertebrate retina”. Experimental Eye Research. 69 (5): 491–503. doi:10.1006/exer.1999.0724. PMID 10548469.
- Jimbo T, Kawasaki Y, Koyama R, Sato R, Takada S, Haraguchi K, Akiyama T (Apr 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.
- Baker SA, Freeman K, Luby-Phelps K, Pazour GJ, Besharse JC (Sep 2003). “IFT20 links kinesin II with a mammalian intraflagellar transport complex that is conserved in motile flagella and sensory cilia”. The Journal of Biological Chemistry. 278 (36): 34211–8. doi:10.1074/jbc.M300156200. PMID 12821668.
- Imamura T, Huang J, Usui I, Satoh H, Bever J, Olefsky JM (Jul 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.
- Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (Jul 2004). “Functional proteomics mapping of a human signaling pathway”. Genome Research. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
- Haraguchi K, Hayashi T, Jimbo T, Yamamoto T, Akiyama T (Feb 2006). “Role of the kinesin-2 family protein, KIF3, during mitosis”. The Journal of Biological Chemistry. 281 (7): 4094–9. doi:10.1074/jbc.M507028200. PMID 16298999.
- Wu Y, Dai XQ, Li Q, Chen CX, Mai W, Hussain Z, Long W, Montalbetti N, Li G, Glynne R, Wang S, Cantiello HF, Wu G, Chen XZ (Nov 2006). “Kinesin-2 mediates physical and functional interactions between polycystin-2 and fibrocystin”. Human Molecular Genetics. 15 (22): 3280–92. doi:10.1093/hmg/ddl404. PMID 17008358.