2f86

From Proteopedia

(Difference between revisions)

Revision as of 10:44, 3 August 2017

The Association Domain of C. elegans CaMKII

Structural highlights

2f86 is a 7 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Calcium/calmodulin-dependent protein kinase, with EC number 2.7.11.17
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KCC2D_CAEEL] Acts in the signaling of a variety of pathways and processes. Phosphorylates 'Ser-319' of daf-16 in response to stress signals, such as heat, starvation and oxidation, which plays a role in prolonging lifespan. Required for viability under chronic osmotic stress in which it acts downstream of osr-1. Has roles in locomotion, oocyte maturation, brood size, egg laying, defecation, meiotic maturation and neuronal cell fate specification. Required for the regulation of synaptic density and neuromuscular junction morphology. Regulates the synaptic trafficking of glr-1. Bidirectional modulator of neurotransmitter release with negative modulatory effects mainly mediated via slo-1 activation. Involved in activation of ADF neurons and increased tph-1 transcription following exposure to pathogenic bacteria which leads to learned olfactory aversion to the bacteria. Implicated in the muscle regulation of spicule protraction. In conjunction with egl-2 has a role in the suppression of mating behavior under food deprivation to encourage foraging. Involved in restricting str-2 expression to only one of the two AWC neurons. May suppress the functional response to an internal pacemaker, perhaps by modulating the activity of the IP3 receptor.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10] ^[11] ^[12] ^[13] ^[14]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Ca2+/calmodulin activated protein kinase II (CaMKII) is an oligomeric protein kinase with a unique holoenyzme architecture. The subunits of CaMKII are bound together into the holoenzyme by the association domain, a C-terminal region of approximately 140 residues in the CaMKII polypeptide. Single particle analyses of electron micrographs have suggested previously that the holoenyzme forms a dodecamer that contains two stacked 6-fold symmetric rings. In contrast, a recent crystal structure of the isolated association domain of mouse CaMKIIalpha has revealed a tetradecameric assembly with two stacked 7-fold symmetric rings. In this study, we have determined the crystal structure of the Caenorhabditis elegans CaMKII association domain and it too forms a tetradecamer. We also show by electron microscopy that in its fully assembled form the CaMKII holoenzyme is a dodecamer but without the kinase domains, either from expression of the isolated association domain in bacteria or following their removal by proteolysis, the association domains form a tetradecamer. We speculate that the holoenzyme is held in its 6-fold symmetric state by the interactions of the N-terminal approximately 1-335 residues and that the removal of this region allows the association domain to convert into a more stable 7-fold symmetric form.

Oligomerization states of the association domain and the holoenyzme of Ca2+/CaM kinase II.,Rosenberg OS, Deindl S, Comolli LR, Hoelz A, Downing KH, Nairn AC, Kuriyan J FEBS J. 2006 Feb;273(4):682-94. PMID:16441656^[15]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Troemel ER, Sagasti A, Bargmann CI. Lateral signaling mediated by axon contact and calcium entry regulates asymmetric odorant receptor expression in C. elegans. Cell. 1999 Nov 12;99(4):387-98. PMID:10571181
↑ Bandyopadhyay J, Lee J, Lee J, Lee JI, Yu JR, Jee C, Cho JH, Jung S, Lee MH, Zannoni S, Singson A, Kim DH, Koo HS, Ahnn J. Calcineurin, a calcium/calmodulin-dependent protein phosphatase, is involved in movement, fertility, egg laying, and growth in Caenorhabditis elegans. Mol Biol Cell. 2002 Sep;13(9):3281-93. PMID:12221132 doi:http://dx.doi.org/10.1091/mbc.E02-01-0005
↑ Solomon A, Bandhakavi S, Jabbar S, Shah R, Beitel GJ, Morimoto RI. Caenorhabditis elegans OSR-1 regulates behavioral and physiological responses to hyperosmotic environments. Genetics. 2004 May;167(1):161-70. PMID:15166144
↑ Umemura T, Rapp P, Rongo C. The role of regulatory domain interactions in UNC-43 CaMKII localization and trafficking. J Cell Sci. 2005 Aug 1;118(Pt 15):3327-38. PMID:16079277 doi:10.1242/jcs.02457
↑ Corrigan C, Subramanian R, Miller MA. Eph and NMDA receptors control Ca2+/calmodulin-dependent protein kinase II activation during C. elegans oocyte meiotic maturation. Development. 2005 Dec;132(23):5225-37. Epub 2005 Nov 2. PMID:16267094 doi:http://dx.doi.org/10.1242/dev.02083
↑ Liu Q, Chen B, Ge Q, Wang ZW. Presynaptic Ca2+/calmodulin-dependent protein kinase II modulates neurotransmitter release by activating BK channels at Caenorhabditis elegans neuromuscular junction. J Neurosci. 2007 Sep 26;27(39):10404-13. PMID:17898212 doi:10.1523/JNEUROSCI.5634-06.2007
↑ LeBoeuf B, Gruninger TR, Garcia LR. Food deprivation attenuates seizures through CaMKII and EAG K+ channels. PLoS Genet. 2007 Sep;3(9):1622-32. Epub 2007 Jul 30. PMID:17941711 doi:http://dx.doi.org/10.1371/journal.pgen.0030156
↑ Nehrke K, Denton J, Mowrey W. Intestinal Ca2+ wave dynamics in freely moving C. elegans coordinate execution of a rhythmic motor program. Am J Physiol Cell Physiol. 2008 Jan;294(1):C333-44. Epub 2007 Oct 17. PMID:17942636 doi:10.1152/ajpcell.00303.2007
↑ LeBoeuf B, Guo X, Garcia LR. The effects of transient starvation persist through direct interactions between CaMKII and ether-a-go-go K+ channels in C. elegans males. Neuroscience. 2011 Feb 23;175:1-17. doi: 10.1016/j.neuroscience.2010.12.002. Epub, 2010 Dec 9. PMID:21145946 doi:http://dx.doi.org/10.1016/j.neuroscience.2010.12.002
↑ Chang C, Hsieh YW, Lesch BJ, Bargmann CI, Chuang CF. Microtubule-based localization of a synaptic calcium-signaling complex is required for left-right neuronal asymmetry in C. elegans. Development. 2011 Aug;138(16):3509-18. doi: 10.1242/dev.069740. Epub 2011 Jul 19. PMID:21771813 doi:http://dx.doi.org/10.1242/dev.069740
↑ Wani KA, Catanese M, Normantowicz R, Herd M, Maher KN, Chase DL. D1 dopamine receptor signaling is modulated by the R7 RGS protein EAT-16 and the R7 binding protein RSBP-1 in Caenoerhabditis elegans motor neurons. PLoS One. 2012;7(5):e37831. doi: 10.1371/journal.pone.0037831. Epub 2012 May 21. PMID:22629462 doi:http://dx.doi.org/10.1371/journal.pone.0037831
↑ Qin Y, Zhang X, Zhang Y. A neuronal signaling pathway of CaMKII and Gqalpha regulates experience-dependent transcription of tph-1. J Neurosci. 2013 Jan 16;33(3):925-35. doi: 10.1523/JNEUROSCI.2355-12.2013. PMID:23325232 doi:http://dx.doi.org/10.1523/JNEUROSCI.2355-12.2013
↑ Caylor RC, Jin Y, Ackley BD. The Caenorhabditis elegans voltage-gated calcium channel subunits UNC-2 and UNC-36 and the calcium-dependent kinase UNC-43/CaMKII regulate neuromuscular junction morphology. Neural Dev. 2013 May 10;8:10. doi: 10.1186/1749-8104-8-10. PMID:23663262 doi:http://dx.doi.org/10.1186/1749-8104-8-10
↑ Tao L, Xie Q, Ding YH, Li ST, Peng S, Zhang YP, Tan D, Yuan Z, Dong MQ. CAMKII and Calcineurin regulate the lifespan of Caenorhabditis elegans through the FOXO transcription factor DAF-16. Elife. 2013 Jun 25;2:e00518. doi: 10.7554/eLife.00518. PMID:23805378 doi:http://dx.doi.org/10.7554/eLife.00518
↑ Rosenberg OS, Deindl S, Comolli LR, Hoelz A, Downing KH, Nairn AC, Kuriyan J. Oligomerization states of the association domain and the holoenyzme of Ca2+/CaM kinase II. FEBS J. 2006 Feb;273(4):682-94. PMID:16441656 doi:10.1111/j.1742-4658.2005.05088.x

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2f86"

@@ Line 1: / Line 1: @@
 ==The Association Domain of C. elegans CaMKII==
 <StructureSection load='2f86' size='340' side='right' caption='[[2f86]], [[Resolution|resolution]] 2.64&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2f86]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F86 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2f86]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F86 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f86 OCA], [http://pdbe.org/2f86 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f86 RCSB], [http://www.ebi.ac.uk/pdbsum/2f86 PDBsum]</span></td></tr>
+</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium/calmodulin-dependent_protein_kinase Calcium/calmodulin-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.17 2.7.11.17] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f86 OCA], [http://pdbe.org/2f86 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f86 RCSB], [http://www.ebi.ac.uk/pdbsum/2f86 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2f86 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/KCC2D_CAEEL KCC2D_CAEEL]] Acts in the signaling of a variety of pathways and processes. Phosphorylates 'Ser-319' of daf-16 in response to stress signals, such as heat, starvation and oxidation, which plays a role in prolonging lifespan. Required for viability under chronic osmotic stress in which it acts downstream of osr-1. Has roles in locomotion, oocyte maturation, brood size, egg laying, defecation, meiotic maturation and neuronal cell fate specification. Required for the regulation of synaptic density and neuromuscular junction morphology. Regulates the synaptic trafficking of glr-1. Bidirectional modulator of neurotransmitter release with negative modulatory effects mainly mediated via slo-1 activation. Involved in activation of ADF neurons and increased tph-1 transcription following exposure to pathogenic bacteria which leads to learned olfactory aversion to the bacteria. Implicated in the muscle regulation of spicule protraction. In conjunction with egl-2 has a role in the suppression of mating behavior under food deprivation to encourage foraging. Involved in restricting str-2 expression to only one of the two AWC neurons. May suppress the functional response to an internal pacemaker, perhaps by modulating the activity of the IP3 receptor.<ref>PMID:10571181</ref> <ref>PMID:12221132</ref> <ref>PMID:15166144</ref> <ref>PMID:16079277</ref> <ref>PMID:16267094</ref> <ref>PMID:17898212</ref> <ref>PMID:17941711</ref> <ref>PMID:17942636</ref> <ref>PMID:21145946</ref> <ref>PMID:21771813</ref> <ref>PMID:22629462</ref> <ref>PMID:23325232</ref> <ref>PMID:23663262</ref> <ref>PMID:23805378</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 28: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Caeel]]
+[[Category: Calcium/calmodulin-dependent protein kinase]]
 [[Category: Kuriyan, J]]
 [[Category: Rosenberg, O S]]

2f86

From Proteopedia

Revision as of 10:44, 3 August 2017

The Association Domain of C. elegans CaMKII

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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