Kinesin

From Proteopedia

(Difference between revisions)

Current revision

1 Function
2 Disease
3 Structural highlights
4 3D Structures of Kinesin

Function

Kinesins are eukaryotic motor proteins which move along microtubules^[1]. Kinesin (KIF) is a dimer consisting of 2 heavy chains and two light chains. The heavy chain contains the N-terminal globular motor domain (MD) residues 1-375, responsible for the motor activity of kinesin, a central flexible neck linker (FNL) coiled-coil stalk which intertwines to form the dimer and a small globular C-terminal domain which interacts with other proteins like the kinesin light chain. The light chain (KLC) forms the tail region. The KLC contains a cargo binding domain which is called TPR (Tetratricopeptide repeat). The KIFs are named by their gene number. KIF are organized into 14 families named kinesin-1 to kinesin-14. KIF contains a forkhead-associated domain (FHA) which is involved in phosphopeptide recognition.

KIF1A transports organelles along axonal microtubules.
KIF1C and KIF2 are plus-ended directed microtubule motors.
KIF2C, KIF22 and KIF3B are plus-ended directed microtubule motors in mitotic cells
KIF13B transports VEGFR2 from the Golgi to the endothelial cell surface.
KIF16B is plus-ended directed microtubule motor involved in endosome transport and receptor recycling.
KIFC1 transports DNA molecules along cytoskeleton filaments.
Kar3 is kinesin protein in yeast.
Eg5 or KIF11 is a kinesin (See Kinesin-5) which participates in mitosis.
NOD is a Drosophila chromosome-associated kinesin.

Disease

Mutations in KIF5A are involved in hereditary spastic paraplegia^[2]. Mutation in KIF1B is the cause of Charcot-Marie-Tooth disease ^[3]. Mutations in KIF22 cause spondyloepimetaphyseal dysplasia^[4].

Structural highlights

. Water molecules shown as red spheres. Residue . Arg216 pivots to enable release or the phosphate release. in the KIF 'closed-state' before the Mg-ADP release. Binding of β-tubulin to KIF releases the latch, enabling the KIF conformation change and detaching KIF from the microtubule and enabling the next movement cycle^[5].

3D Structures of Kinesin

Kinesin 3D Structures

References

↑ Hirokawa N, Noda Y, Tanaka Y, Niwa S. Kinesin superfamily motor proteins and intracellular transport. Nat Rev Mol Cell Biol. 2009 Oct;10(10):682-96. doi: 10.1038/nrm2774. PMID:19773780 doi:http://dx.doi.org/10.1038/nrm2774
↑ Ebbing B, Mann K, Starosta A, Jaud J, Schols L, Schule R, Woehlke G. Effect of spastic paraplegia mutations in KIF5A kinesin on transport activity. Hum Mol Genet. 2008 May 1;17(9):1245-52. doi: 10.1093/hmg/ddn014. Epub 2008 Jan, 18. PMID:18203753 doi:http://dx.doi.org/10.1093/hmg/ddn014
↑ Hirokawa N, Takemura R. Biochemical and molecular characterization of diseases linked to motor proteins. Trends Biochem Sci. 2003 Oct;28(10):558-65. PMID:14559185 doi:http://dx.doi.org/10.1016/j.tibs.2003.08.006
↑ Grosch M, Gruner B, Spranger S, Stutz AM, Rausch T, Korbel JO, Seelow D, Nurnberg P, Sticht H, Lausch E, Zabel B, Winterpacht A, Tagariello A. Identification of a Ninein (NIN) mutation in a family with spondyloepimetaphyseal dysplasia with joint laxity (leptodactylic type)-like phenotype. Matrix Biol. 2013 Oct-Nov;32(7-8):387-92. doi: 10.1016/j.matbio.2013.05.001. Epub, 2013 May 9. PMID:23665482 doi:http://dx.doi.org/10.1016/j.matbio.2013.05.001
↑ Nitta R, Okada Y, Hirokawa N. Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin. Nat Struct Mol Biol. 2008 Oct;15(10):1067-75. Epub 2008 Sep 21. PMID:18806800 doi:10.1038/nsmb.1487

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, David Canner, Joel L. Sussman, Jaime Prilusky

Retrieved from "http://52.214.119.220/wiki/index.php/Kinesin"

Category: Topic Page

@@ Line 3: / Line 3: @@
 == Function ==
-[[Kinesin|Kinesins]] are eukaryotic motor proteins which move along microtubules<ref>PMID:19773780</ref>.  Kinesin (KIF) is a dimer consisting of 2 heavy chains and two light chains.  The heavy chain contains the N-terminal globular motor domain (MD) responsible for the motor activity of kinesin, a central flexible neck linker (FNL) coiled-coil stalk which intertwines to form the dimer and a small globular C-terminal domain which interacts with other proteins like the kinesin light chain.  The light chain (KLC) forms the tail region. The KLC contains a cargo binding domain which is called TPR (Tetratricopeptide repeat).  The KIFs are named by their gene number.  KIF contains a forkhead-associated domain (FHA) which is involved in phosphopeptide recognition.<br />
+[[Kinesin|Kinesins]] are eukaryotic motor proteins which move along microtubules<ref>PMID:19773780</ref>.  Kinesin (KIF) is a dimer consisting of 2 heavy chains and two light chains.  The heavy chain contains the N-terminal globular motor domain (MD) residues 1-375, responsible for the motor activity of kinesin, a central flexible neck linker (FNL) coiled-coil stalk which intertwines to form the dimer and a small globular C-terminal domain which interacts with other proteins like the kinesin light chain.  The light chain (KLC) forms the tail region. The KLC contains a cargo binding domain which is called TPR (Tetratricopeptide repeat).  The KIFs are named by their gene number. KIF are organized into 14 families named kinesin-1  to kinesin-14. KIF contains a forkhead-associated domain (FHA) which is involved in phosphopeptide recognition.<br />
 *'''KIF1A''' transports organelles along axonal microtubules.<br />
 *'''KIF1C''' and '''KIF2''' are plus-ended directed microtubule motors.<br />
@@ Line 27: / Line 27: @@
 </StructureSection>
-== 3D Structures of Kinesin ==
-Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-{{#tree:id=OrganizedByTopic|openlevels=0|
-*Kinesin heavy chain
-**[[4ejq]], [[4egx]] - hKIF1A FHA domain - human<br />
-**[[1bg2]] – hKIF MD<br />
-**[[5lt3]], [[5lt4]], [[5lt2]], [[5lt0]], [[5lt1]] – hKIF1 MD (mutant) <br />
-**[[2g1l]] - hKIF1C FHA domain<br />
-**[[5wdh]] – hKIF1C MD<br />
-**[[2rep]] – hKIFC1 MD<br />
-**[[2eh0]] - hKIF1B FHA domain – NMR<br />
-**[[2heh]], [[4ubf]], [[5y05]] – hKIF2C<br />
-**[[3b6u]], [[3b6v]] – hKIF3B MD<br />
-**[[4a14]] – hKIF7 MD <br />
-**[[2xt3]] – hKIF7 MD (mutant)<br />
-**[[3j2u]] – hKIF10A head domain – Cryo EM<br />
-**[[2cow]] – hKIF13B CAP-gly domain – NMR<br />
-**[[4bn2]] – hKIF15 MD<br />
-**[[2v14]] – hKIF16B<br />
-**[[5d3a]] – hKIF21A coiled coil domain 938-1017  <br />
-**[[2edu]] – hKIF22 C-terminal – NMR<br />
-**[[3bfn]] – hKIF22 MD<br />
-**[[2zfi]], [[2zfj]], [[2zfk]], [[2zfl]], [[2zfm]] – mKIF1A – mouse<br />
-**[[6ign]], [[6igv]] – mKIF5B coiled coil domain 444-566  <br />
-**[[3wrd]] – mKIF5C<br />
-**[[5djo]] – mKIF13A CC1-FHA domain <br />
-**[[5djn]] – mKIF13A coiled-coil domain (mutant)<br />
-**[[3kin]], [[2kin]] – rKIF MD - rat<br />
-**[[6a1z]] – rKIF13B<br />
-**[[6a20]] – rKIF13B (mutant)<br />
-**[[1ry6]] – KIF MD – ''Plasmodium falciparum''<br />
-**[[2ncd]], [[1cz7]] – DmKIF MD non-claret disjuctional (NCD) dimer – ''Drosophila melanogaster'' <br />
-**[[2y5w]], [[2y65]] - DmKIF MD<br />
-**[[2vvg]] – KIF2 MD – ''Giardia intestinalis''<br />
-**[[2owm]] – NcKIF1C MD – ''Neurospora crassa''<br />
-**[[1goj]] – NcKIF MD<br />
-*''Kinesin heavy chain complex with nucleotide''
-**[[2gry]] – hKIF2+ADP<br />
-**[[2h58]], [[5wde]] – hKIFC3+ADP<br />
-**[[3nwn]] – hKIF9+ADP<br />
-**[[3gbj]] – hKIF13B MD+ADP <br />
-**[[2cjo]] – hKIF13+inhibitor 30<br />
-**[[1vfv]], [[1vfw]] – mKIF1A MD+Mg-AMPPNP<br />
-**[[1vfx]] - mKIF1A MD+ADP-Mg-AlFx<br />
-**[[1vfz]] - mKIF1A MD+ADP-Mg-VO4<br />
-**[[1v8j]], [[5xja]], [[5xjb]] – mKIF2C MD+Mg-ADP<br />
-**[[1i5s]] - mKIF2C MD (mutant)+Mg-ADP<br />
-**[[1i6i]] - mKIF2C MD (mutant)+Mg-AMPPCP<br />
-**[[1v8k]] - mKIF2C MD+Mg-AMPPNP<br />
-**[[3zfc]], [[3zfd]] – mKIF4 MD+Mg-AMPPNP<br />
-**[[3x2t]] – mKIF5C + ADP<br />
-**[[5gsy]] – mKIF19A MD + GDP<br />
-**[[5gsz]] – mKIF19A MD + ADP<br />
-**[[3uyq]] – pKIF1A head+AMPPNP – pig<br />
-**[[2hxh]] - pKIF1A head+ADP<br />
-**[[2hxf]] - pKIF1A head+AMPPNP<br />
-*''Kinesin heavy chain complex with protein''
-**[[4hna]], [[4lnu]] – hKIF1 + Tubulin + designed ankyrin repeat protein + Mg-ADP + GDP + GTP + AlF4<br />
-**[[4uxy]] – hKIF1 MD + Tubulin + GDP + GTP – Cryo EM<br />
-**[[4uy0]] – hKIF1 MD + Tubulin + GDP + GTP + ADP – Cryo EM<br />
-**[[2p4n]] – hKIF+ Tubulin  – EM docking<br />
-**[[1mkj]] – hKIF MD+docked FNL<br />
-**[[5mio]] – hKIF2C MD + Tubulin <br />
-**[[3fm8]] – hKIF13B FHA domain + centaurin-alpha-1<br />
-**[[3md8]] – hKIF13B FHA domain + centaurin-alpha-1 + IP4<br />
-**[[3vhx]] – hKIF23 794-911 + ADP-ribosylation factor 6 <br />
-**[[2wbe]] – cKIF MD+FNL+Tubulin +AMPPNP – bovine <br />
-**[[3edl]] – cKIF MD+ Tubulin – EM<br />
-**[[1ia0]] – pKIF1A MD+Tubulin +ATP <br />
-**[[4atx]] - rKIF MD+ Tubulin  – Cryo EM<br />
-**[[3j6h]] – mKIF5C MD+Mg-GTP + G2P + tubulin <br />
-**[[3j8x]], [[3j8y]] – mKIF5C MD+ GTP + GDP + tubulin<br />
-**[[5nd3]] – mKIF20A MD + tubulin <br />
-**[[5nd2]], [[5nd4]] – mKIF20A MD + tubulin + ADP <br />
-**[[5nd7]] – mKIF20A MD + tubulin + AMPPNP <br />
-**[[5lef]] – mKIF20A residues 603-665 + RAB-6 <br />
-**[[1n6m]] – DmKIF MD+FNL<br />
-*Kinesin light chain (KLC)
-**[[5oj8]] – hKLC1 TPR domain <br />
-**[[3edt]] – hKLC2<br />
-**[[3ceq]], [[3nf1]] – hKLC2 TPR domain<br />
-**[[6f9i]] – hKLC2 + clcytenin peptide <br />
-**[[6fv0]] – mKLC1 TPR domain + nanobody<br />
-**[[5ojf]] – mKLC2 TPR domain <br />
-**[[3zfw]], [[5fjy]], [[6ejn]] - mKLC2 TPR domain + peptide<br />
-*Kinesin-3 motor domain
-**[[4uxo]], [[4uxp]], [[4uxr]], [[4uxs]], [[4uxt]] - KIF + tubulin 1B, 2B chains + GDP + GTP – bovine – Cryo EM <br />
-**[[5zbs]] – rKIF13B (mutant)<br />
-**[[5zbr]] – rKIF13B + AMPPNP<br />
-**[[5b64]] – mKIF13B + MAGUK<br />
-*Kinesin-5 motor domain
-**[[4b7b]] - hKIF11 (mutant) + ADP + Co + Cd <br />
-**[[3ken]], [[2wog]], [[2x2r]], [[2xae]], [[4bbg]] - hKIF11 +S-trityl-L-cysteine derivative + ADP + Mg<br />
-**[[3wpn]] - hKIF11 +inhibitor  <br />
-**[[2uyi]], [[2uym]], [[2gm1]], [[2pg2]], [[2fme]], [[2x7d]], [[2x7c]], [[2ieh]], [[3cjo]], [[2g1q]], [[2fl2]], [[2fl6]], [[1yrs]], [[2q2y]], [[2fky]], [[2q2z]], [[3k3b]], [[2x7e]], [[4a50]], [[4a51]], [[3zcw]] - hKIF11+inhibitor +ADP + Mg<br />
-**[[4bxn]], [[4as7]] - hKIF11+inhibitor +ADP + Cd<br />
-**[[3l9h]] - hKIF11+inhibitor +ADP <br />
-**[[4zhi]] – hKIF11 MD +ADP<br />
-**[[1x88]], [[1q0b]] - hKIF11 +Mg + ADP+monastrol <br />
-**[[4ap0]], [[4a5y]] - hKIF11 +MgADP + ispinesib + Mg<br />
-**[[3hqd]] - hKIF11 +AMPPNP+Mg<br />
-**[[1ii6]], [[4a1z]], [[4a28]] - hKIF11 +ADP+Mg<br />
-**[[4zca]] - hKIF11 (mutant) +ADP+Mg<br />
-**[[3k5e]] - hKIF11 +ADP+enastrol + Mg<br />
-**[[4aqv]], [[4aqw]] – hKIF11 (mutant) + tubulin + GDP + GTP + Mg – Cryo EM<br />
-**[[4ck5]], [[4ck6]], [[4ck7]] – hKIF11 (mutant) + tubulin + ADP + GDP + GTP + Mg – Cryo EM<br />
-**[[4pxt]], [[4pxu]] – DmKIF (mutant)<br />
-**[[5m5i]], [[5m5l]], [[5m5m]], [[5m5n]], [[5m5o]] – KIF + tubulin + GDP + GTP + ANP + taxol – fission yeast – Cryo EM<br />
-**[[5mm4]], [[5mm7]] – KIF + tubulin + GDP + GTP + ANP + taxol – Ustilago maydis – Cryo EM<br />
-*Kinesin-6
-**[[5x3e]] - KLP MD - ''Caenorhabditis elegans''<br />
-*Kinesin-8
-**[[3lre]] - hKIF18A MD <br />
-**[[5oam]] - hKIF18A MD + tubulin + GTP<br />
-**[[5ocu]] - hKIF18A MD + tubulin + GTP + GDP + ANP<br />
-**[[5ogc]] - hKIF18A MD + tubulin + GTP + GDP + taxol<br />
-*Kinesin-14
-**[[1f9t]], [[1f9u]], [[1f9v]], [[1f9w]], [[3kar]] - yKar3 MD (mutant) - yeast<br />
-**[[4etp]] - yKar3 MD (mutant) + VIK1<br />
-**[[3l1c]] – DmNCD (mutant)
-*KCBP
-**[[3h4s]] – KCBP+ADP+Mg – ''Arabidopsis thaliana''<br />
-*NOD
-**[[3dc4]] – DmNOD catalytic core domain+ADP<br />
-**[[3dcb]] - DmNOD catalytic core domain+AMPPNP<br />
-**[[3dco]] - DmNOD catalytic core domain+ cTubulin A+cTubulin B<br />
-}}
 == References ==
 <references/>
 [[Category:Topic Page]]

Kinesin

From Proteopedia

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Contents

Function

Disease

Structural highlights

3D Structures of Kinesin

References

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