gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Cullin-associated and neddylation-dissociated 1

CAND1, TIP120A, TIP120
interacts with TATA-binding protein and may be involved in transcription regulation [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: Ubiquitin, Cullin, NEDD8, SCF, CAN
Papers on CAND1
Comprehensive assessment of cancer missense mutation clustering in protein structures.
Getz et al., Cambridge, United States. In Proc Natl Acad Sci U S A, Nov 2015
The approach can also be used to search for proteins with an enrichment of mutations at binding interfaces with a protein, nucleic acid, or small molecule partner.
Characterisation of the Cullin-3 mutation that causes a severe form of familial hypertension and hyperkalaemia.
Kurz et al., Zürich, Switzerland. In Embo Mol Med, Oct 2015
Instead, CUL3(Δ403-459) auto-ubiquitylates and loses interaction with two important Cullin regulators: the COP9-signalosome and CAND1.
CAND1 exchange factor promotes Keap1 integration into cullin 3-RING ubiquitin ligase during adipogenesis.
Naumann et al., Magdeburg, Germany. In Int J Biochem Cell Biol, Sep 2015
Here, we show that the differentiation of LiSa-2 preadipocytes is associated with an increase of cullin-associated and neddylation-dissociated 1 (CAND1), COP9 signalosome (CSN), neddylated cullin 3 (Cul3) and the BTB protein Keap1.
The cullin-4 complex DCDC does not require E3 ubiquitin ligase elements to control heterochromatin in Neurospora crassa.
Selker et al., Eugene, United States. In Eukaryot Cell, 2015
Moreover, the RING domain protein RBX1 and a segment of the CUL4 C terminus that normally interacts with RBX1, the E2 ligase, CAND1, and CSN are dispensable for DNA methylation and heterochromatin formation by DCDC.
SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of SCCRO (DCUN1D1).
Singh et al., New York City, United States. In J Biol Chem, 2015
We found that although SCCRO3 binds to CAND1, cullins, and ROC1, it does not efficiently bind to Ubc12, promote cullin neddylation, or conform to the reaction processivity paradigms, suggesting that SCCRO3 does not have E3 activity.
CBS9106-induced CRM1 degradation is mediated by cullin ring ligase activity and the neddylation pathway.
Kawabe et al., Numazu, Japan. In Mol Cancer Ther, 2014
MLN4924 also attenuated CBS9106-induced nuclear accumulation of Ran-binding protein 1 (RanBP1), cell growth inhibition, and apoptosis.
Selecting key genes associated with osteosarcoma based on a differential expression network.
Jia et al., Jinan, China. In Genet Mol Res, 2014
Six hub genes (APP, UBC, CAND1, RPA, YWHAG, and NEDD8) were discovered; of these, two genes (UBC and RPA) were also found to be disease genes.
The NEDD8 modification pathway in plants.
Schwechheimer et al., Freising, Germany. In Front Plant Sci, 2013
In turn, NEDD8 deconjugation destabilizes the cullin RING ligase complex allowing for the exchange of substrate recognition subunits via the exchange factor CAND1.
Negative regulation of NEDD8 conjugation pathway by novel molecules and agents for anticancer therapy.
Kamitani et al., Ōsaka, Japan. In Curr Pharm Des, 2012
COP9 signalosome, CAND1, inactive mutant of Ubc12 and NUB1/NUB1L) and clarifies possible strategies for targeting the NEDD8 cascade in cancer cells.
Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration.
Bahn et al., Cambridge, United Kingdom. In J Proteome Res, 2012
A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.
COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding.
Burstein et al., Dallas, United States. In J Biol Chem, 2011
COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding.
Structural regulation of cullin-RING ubiquitin ligase complexes.
Schulman et al., Memphis, United States. In Curr Opin Struct Biol, 2011
Recent structural studies have revealed numerous ways in which CRL E3 ligase activities are controlled, including multimodal E3 ligase activation by covalent attachment of the ubiquitin-like protein NEDD8, inhibition of CRL assembly/activity by CAND1, and several mechanisms of regulated substrate recruitment.
Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics.
Harper et al., Boston, United States. In Cell, 2011
Current models suggest that CRL complexes are controlled by cycles of CRL deneddylation and CAND1 binding.
Regulation of the Nrf2-Keap1 antioxidant response by the ubiquitin proteasome system: an insight into cullin-ring ubiquitin ligases.
Zhang et al., Tucson, United States. In Antioxid Redox Signal, 2011
They are regulated by neddylation/deneddylation, ubiquitination/deubiquitination, CAND1-assisted complex assembly/disassembly, and subunit dimerization.
miR-148a is an androgen-responsive microRNA that promotes LNCaP prostate cell growth by repressing its target CAND1 expression.
Inoue et al., Tokyo, Japan. In Prostate Cancer Prostatic Dis, 2010
miR-148a is an androgen-responsive microRNA that promotes LNCaP prostate cell growth by repressing its target CAND1 expression.
Regulation of cullin RING E3 ubiquitin ligases by CAND1 in vivo.
Hagen et al., Singapore, Singapore. In Plos One, 2010
CAND1 does not function by sequestering cullins in vivo to prevent substrate receptor autoubiquitination and is likely to regulate cullin RING ligase activity via alternative mechanisms
SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation.
Singh et al., New York City, United States. In J Biol Chem, 2008
SCCRO recruits Ubc12 approximately NEDD8 to the CAND1-Cul1-ROC1 complex but that this is not sufficient to dissociate or overcome the inhibitory effects of CAND1 on cullin neddylation
Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation.
Schulman et al., Memphis, United States. In Cell, 2008
Covalent attachment of the ubiquitin-like protein NEDD8 to a conserved C-terminal domain (ctd) lysine stimulates CRL ubiquitination activity and prevents binding of the inhibitor CAND1.
Regulation of cullin RING ligases.
Callis et al., Davis, United States. In Annu Rev Plant Biol, 2007
CULLIN-ASSOCIATED NEDD8-DISSOCIATED 1 (CAND1) interacts with CRLs, affecting both rubylation and derubylation.
Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage.
Xiong et al., Chapel Hill, United States. In Nat Cell Biol, 2004
As with SKP1-CUL1, the DDB1-CUL4A association is negatively regulated by the cullin-associated and neddylation-dissociated protein, CAND1.
share on facebooktweetadd +1mail to friends