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

Tumor protein D52-like 1

D53, TPD52L1, TPD52L2, hD53
This gene encodes a member of the tumor protein D52 (TPD52) family. The encoded protein contains a coiled-coil domain and may form homo- or hetero-dimer with TPD52 family members. The protein is reported to be involved in cell proliferation and calcium signaling. It also interacts with the mitogen-activated protein kinase kinase kinase 5 (MAP3K5/ASK1) and positively regulates MAP3K5-induced apoptosis. Multiple alternatively spliced transcript variants have been observed, but the full-length nature of some variants has not yet been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: HAD, CAN, ACID, V1a, POLYMERASE
Papers on D53
Coq7p relevant residues for protein activity and stability.
Barros et al., São Paulo, Brazil. In Biochimie, Dec 2015
Here we indicate a group of Coq7p residues that modulate protein activity: D53, R57, V111 and S114.
SMAX1-LIKE/D53 Family Members Enable Distinct MAX2-Dependent Responses to Strigolactones and Karrikins in Arabidopsis.
Nelson et al., Cambridge, United Kingdom. In Plant Cell, Nov 2015
Recent studies suggest that the homologous SUPPRESSOR OF MAX2 1 (SMAX1) in Arabidopsis and DWARF53 (D53) in rice (Oryza sativa) are downstream targets of MAX2.
Strigolactone Signaling in Arabidopsis Regulates Shoot Development by Targeting D53-Like SMXL Repressor Proteins for Ubiquitination and Degradation.
Li et al., Beijing, China. In Plant Cell, Nov 2015
In rice (Oryza sativa), SL signaling requires the degradation of DWARF53 (D53), mediated by a complex including D14 and D3, but in Arabidopsis thaliana, the components and mechanism of SL signaling involving the D3 ortholog MORE AXILLARY GROWTH2 (MAX2) are unknown.
TPD52 expression increases neutral lipid storage within cultured cells.
Byrne et al., Westmead, Australia. In J Cell Sci, Oct 2015
We found increased lipid droplet numbers in BALB/c 3T3 cell lines stably expressing TPD52, compared with control and TPD52L1-expressing cell lines.
Structural Requirements of Strigolactones for Shoot Branching Inhibition in Rice and Arabidopsis.
Yamaguchi et al., Sakai, Japan. In Plant Cell Physiol, Jun 2015
Moreover, yeast two-hybrid experiments using a possible SL receptor, DWARF14 (D14), and a repressor in the SL signaling pathway, DWARF53 (D53), showed that D14 can interact with D53 in the presence of (2'R) stereoisomers of SLs, but not (2'S) stereoisomers, suggesting that the stereostructure of SLs is crucial for the interaction of these proteins.
Tumor protein D52-like 2 accelerates gastric cancer cell proliferation in vitro.
Cai et al., Shanghai, China. In Cancer Biother Radiopharm, Apr 2015
Tumor protein D52-like 2 (TPD52L2) has been commonly described as a protein involved in tumorigenesis, according to its name.
Tumor protein D52-like 2 contributes to proliferation of breast cancer cells.
Wu et al., Changchun, China. In Cancer Biother Radiopharm, Feb 2015
Tumor protein D52-like 2 (TPD52L2) is one member of the TPD52 family, which has been shown to function in mediating cell proliferation, apoptosis, and vehicle trafficking.
Evidence that KARRIKIN-INSENSITIVE2 (KAI2) Receptors may Perceive an Unknown Signal that is not Karrikin or Strigolactone.
Nelson et al., Athens, United States. In Front Plant Sci, 2014
KAI2 and D14 act in parallel signaling pathways that share a requirement for the F-box protein MAX2, but produce distinct growth responses by regulating different members of the SMAX1-LIKE/D53 family.
Lentivirus-mediated TPD52L2 depletion inhibits the proliferation of liver cancer cells in vitro.
Zhou et al., Shanghai, China. In Int J Clin Exp Med, 2014
Tumor protein D52-like 2, known as hD54 in previous studies (TPD52L2), is a member of TPD52 family which has been implicated in multiple human cancers.
Signalling and responses to strigolactones and karrikins.
Li et al., Australia. In Curr Opin Plant Biol, 2014
D3 mediates SL-dependent ubiquitination and proteolysis of DWARF53 (D53) protein, thought to be involved in the control of gene expression, while a related protein SUPPRESSOR OF MAX2-1 (SMAX1) is implicated in the response to KAR in Arabidopsis.
The karrikin response system of Arabidopsis.
Smith et al., Australia. In Plant J, 2014
The karrikin response requires a newly discovered protein (SMAX1), a homologue of rice protein D53 that is required for the strigolactone response.
DWARF 53 acts as a repressor of strigolactone signalling in rice.
Li et al., Beijing, China. In Nature, 2014
Here we report the characterization of a dominant SL-insensitive rice (Oryza sativa) mutant dwarf 53 (d53) and the cloning of D53, which encodes a substrate of the SCF(D3) ubiquitination complex and functions as a repressor of SL signalling.
D14-SCF(D3)-dependent degradation of D53 regulates strigolactone signalling.
Wan et al., Nanjing, China. In Nature, 2014
Here we show that DWARF 53 (D53) acts as a repressor of SL signalling and that SLs induce its degradation.
Expression of tumor protein D52-like genes in childhood leukemia at diagnosis: clinical and sample considerations.
Byrne et al., Sydney, Australia. In Leuk Res, 2006
The results indicate that tumor protein D52-like 1 genes are not ubiquitously expressed in leukemic bone marrow in children, and that RNA sample parameters may influence measures of gene expression more than commonly appreciated.
Positive regulation of apoptosis signal-regulating kinase 1 by hD53L1.
Park et al., Taejŏn, South Korea. In J Biol Chem, 2004
a member of the tumor protein D52 family involved in cell proliferation and calcium signaling, up-regulates the ASK1-induced apoptosis [D53L1]
Alternative splicing as a mechanism for regulating 14-3-3 binding: interactions between hD53 (TPD52L1) and 14-3-3 proteins.
Byrne et al., Westmead, Australia. In J Mol Biol, 2003
These results identify 14-3-3 proteins as partners for hD53, and alternative splicing as a mechanism for regulating 14-3-3 binding.
Apocrustacyanin C(1) crystals grown in space and on earth using vapour-diffusion geometry: protein structure refinements and electron-density map comparisons.
Helliwell et al., Manchester, United Kingdom. In Acta Crystallogr D Biol Crystallogr, 2003
D53, 231-239], contrary to the case for lysozyme crystals grown in space with liquid-liquid diffusion, i.e. without any major motion during growth [Snell et al. (1995), Acta Cryst.
Error estimation and bias correction in phase-improvement calculations.
Cowtan, York, United Kingdom. In Acta Crystallogr D Biol Crystallogr, 1999
D53, 371-376] to arbitrary density-modification techniques.
share on facebooktweetadd +1mail to friends