KLHL42 (12p11.22), KLHDC5, Ctb9. Cul3 adaptori p60/kataniinin poistamisessa

https://www.ncbi.nlm.nih.gov/gene/57542

Also known as

Ctb9; KLHDC5

Expression

Ubiquitous expression in brain (RPKM 7.6), endometrium (RPKM 5.0) and 25 other tissues See more

Preferred Names

kelch-like protein 42

Names

cullin-3-binding protein 9

kelch domain containing 5

kelch domain-containing protein 5

1. NM_020782.2 → NP_065833.1  kelch-like protein 42
   See identical proteins and their annotated locations for NP_065833.1

   ORIGIN      
           1 msaeemvqir ledrcypvsk rklieqsdyf ralyrsgmre alsqeaggpe vqqlrglsap
          61 glrlvldfin aggaregwll gprgekgggv dedeemdevs llselveaas flqvtsllql
         121 llsqvrlnnc lemyrlaqvy glpdlqeacl rfmvvhfhev lckpqfhllg sppqapgdvs
         181 lkqrlrearm tgtpvlvalg dflggplaph pyqgeppsml ryeemterwf plannlppdl
         241 vnvrgygsai ldnylfivgg yritsqeisa ahsynpstne wlqvasmnqk rsnfklvavn
         301 sklyaiggqa vsnvecynpe qdawnfvapl pnplaefsac eckgkiyvig gyttrdrnmn
         361 ilqycpssdm wtlfetcdvh irkqqmvsve etiyivggcl helgpnrrss qsedmltvqs
         421 yntvtrqwly lkentsksgl nltcalhndg iyimsrdvtl stslehrvfl kynifsdswe
         481 afrrfpafgh nllvsslylp nkaet
   //

   Status: VALIDATED

   Source sequence(s)

   AC009511

   Conserved Domains (4) summary

   cd14735
   Location:129 → 169

   BACK_Kelch; BTB-And-C-terminal-Kelch (BACK) domain of Kelch-like proteins

   sd00038
   Location:244 → 287

   Kelch; KELCH repeat [structural motif]

   cl02518
   Location:7 → 69

   BTB; BTB/POZ domain

   cl28614
   Location:210 → 497

   BTB; Broad-Complex, Tramtrack and Bric a brac

1. The Cul3/Klhdc5 E3 ligase regulates p60/katanin and is required for normal mitosis in mammalian cells. Cummings CM, et al. J Biol Chem, 2009 Apr 24. PMID 19261606, Free PMC ArticleAbstract
   The proper regulation of factors involved in mitosis is crucial to ensure normal cell division. Levels and activities of proteins are regulated in many ways, one of which is ubiquitin-mediated protein degradation. E3 ubiquitin ligases are involved in targeting specific substrates for degradation by facilitating their ubiquitination. In seeking to elucidate additional biological roles for Cul3 we performed a two-hybrid screen and identified Ctb9/KLHDC5 as a Cul3-interacting protein. Overexpression of Ctb9/KLHDC5 resulted in an increase in microtubule density as well as persistent microtubule bridges between post-mitotic cells. Conversely, down-regulation of Ctb9/KLHDC5 showed a pronounced reduction in microtubule density. Based on these observations, we examined the interactions between Cul3, Ctb9/KLHDC5, and the microtubule-severing protein, p60/katanin. Here we show that p60/katanin interacts with a complex consisting of Cul3 and Ctb9/KLHDC5, which results in ubiquitin laddering of p60/katanin. Also, Cul3-deficient cells or Ctb9/KLHDC5-deficient cells show an increase in p60/katanin levels, indicating that Cul3/Ctb9/KLHDC5 is required for efficient p60/katanin removal. We demonstrate a novel regulatory mechanism for p60/katanin that occurs at the level of targeted proteolysis to allow normal mitotic progression in mammalian cells.

   DOI:

   10.1074/jbc.M809374200

2. The ubiquitin conjugating enzyme, UbcM2, engages in novel interactions with components of cullin-3 based E3 ligases. Plafker KS, et al. Biochemistry, 2009 Apr 21. PMID 19256485, Free PMC Article
3. Update on the Kelch-like (KLHL) gene family. Dhanoa BS, et al. Hum Genomics, 2013 May 15. PMID 23676014, Free PMC Article

KATANIINI
https://www.researchgate.net/profile/Abhishek_Guha2/publication/249993435/figure/fig2/AS:393169633071114@1470750353747/Regulators-of-Katanin_Q320.jpg