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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Calcium binding and coiled-coil domain 2

The protein encoded by this gene is a subunit of nuclear domain 10 (ND10) bodies. ND10 bodies are nuclear domains appearing immunohistochemically as ten dots per nucleus. They are believed to be associated with the nuclear matrix on the basis of their resistance to nuclease digestion and salt extraction. ND10 proteins are removed from the nucleus by herpes simplex virus-1 infection and may have a role in viral life cycles. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, LC3, CAN, PML, Sp100
Papers using NDP52 antibodies
NBR1 is a new PB1 signalling adapter in Th2 differentiation and allergic airway inflammation in vivo
Into Takeshi et al., In Cellular and Molecular Life Sciences, 2009
... AL227), anti-BAG3 rabbit polyclonal antibody (Abcam; ab86298), anti-BNIP3L (NIX) rabbit polyclonal antibody (Abcam; ab8399), anti-NDP52 (CALCOCO2) rabbit polyclonal antibody (Abcam; ab68588), anti-Flag M2 monoclonal ...
Papers on NDP52
Unique role for ATG5 in neutrophil-mediated immunopathology during M. tuberculosis infection.
Stallings et al., Saint Louis, United States. In Nature, Jan 2016
The involvement of autophagy has been defined based on studies in cultured cells where M. tuberculosis co-localizes with autophagy factors ATG5, ATG12, ATG16L1, p62, NDP52, BECN1 and LC3 (refs 2-6), stimulation of autophagy increases bacterial killing, and inhibition of autophagy increases bacterial survival.
Molecular basis of ubiquitin recognition by the autophagy receptor CALCOCO2.
Pan et al., Shanghai, China. In Autophagy, Nov 2015
The autophagy receptor CALCOCO2/NDP52 functions as a bridging adaptor and plays an essential role in the selective autophagic degradation of invading pathogens by specifically recognizing ubiquitin-coated intracellular pathogens and subsequently targeting them to the autophagic machinery; thereby it is required for innate immune defense against a range of infectious pathogens in mammals.
The PINK1-PARKIN Mitochondrial Ubiquitylation Pathway Drives a Program of OPTN/NDP52 Recruitment and TBK1 Activation to Promote Mitophagy.
Harper et al., Boston, United States. In Mol Cell, Nov 2015
We report that assembly of ubiquitin chains on mitochondria triggers autophagy adaptor recruitment concomitantly with activation of the TBK1 kinase, which physically associates with OPTN, NDP52, and SQSTM1.
The Autophagy Receptor TAX1BP1 and the Molecular Motor Myosin VI Are Required for Clearance of Salmonella Typhimurium by Autophagy.
Buss et al., Cambridge, United Kingdom. In Plos Pathog, Oct 2015
In this process, selective autophagy receptors, including the myosin VI adaptor proteins optineurin and NDP52, have been shown to recognize cytosolic pathogens.
A variant in the nuclear dot protein 52kDa gene increases the risk for spontaneous bacterial peritonitis in patients with alcoholic liver cirrhosis.
Nischalke et al., Bonn, Germany. In Dig Liver Dis, Oct 2015
We investigated if nuclear dot protein 52kDa (NDP52), a negative regulator of toll-like receptor (TLR) signalling and autophagy adaptor protein, might be involved.
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy.
Youle et al., Bethesda, United States. In Nature, Sep 2015
Using genome editing to knockout five autophagy receptors in HeLa cells, here we show that two receptors previously linked to xenophagy, NDP52 and optineurin, are the primary receptors for PINK1- and parkin-mediated mitophagy.
Emerging themes in bacterial autophagy.
Girardin et al., Toronto, Canada. In Curr Opin Microbiol, Feb 2015
We review the importance of bacterial targeting by ubiquitination, diacylglycerol (DAG) or proteins such as Nod1, Nod2, NDP52, p62, NBR1, optineurin, LRSAM1 and parkin in the process of xenophagy.
A Noncanonical Autophagy Pathway Restricts Toxoplasma gondii Growth in a Strain-Specific Manner in IFN-γ-Activated Human Cells.
Sibley et al., Saint Louis, United States. In Mbio, 2014
Vacuoles containing susceptible strains of T. gondii became ubiquitinated, recruited the adaptors p62 and NDP52, and were decorated with LC3.
Dual function of CALCOCO2/NDP52 during xenophagy.
Faure et al., Lyon, France. In Autophagy, 2014
In infected cells, the autophagy receptor CALCOCO2/NDP52 targets Salmonella Typhimurium to the phagophore membrane by concomitantly interacting with LC3C and binding to ubiquitinated cytosolic bacteria or to LGALS8/GALECTIN 8 adsorbed on damaged vacuoles that contain bacteria.
The role of the selective adaptor p62 and ubiquitin-like proteins in autophagy.
Lőw et al., Budapest, Hungary. In Biomed Res Int, 2013
Selective substrates of autophagy include damaged mitochondria, intracellular pathogens, and even a subset of cytosolic proteins with the help of ubiquitin-binding autophagic adaptors, such as p62/SQSTM1, NBR1, NDP52, and Optineurin.
Myosin VI and its cargo adaptors - linking endocytosis and autophagy.
Buss et al., Cambridge, United Kingdom. In J Cell Sci, 2013
In addition, myosin VI has been shown to be a regulator of the autophagy pathway, because of its ability to link the endocytic and autophagic pathways through interactions with the ESCRT-0 protein Tom1 and the autophagy adaptor proteins T6BP, NDP52 and optineurin.
The role of 'eat-me' signals and autophagy cargo receptors in innate immunity.
Randow et al., Cambridge, United Kingdom. In Curr Opin Microbiol, 2013
The autophagy cargo receptors p62, NDP52 and Optineurin detect incoming bacteria that have become associated with specific 'eat-me' signals such as Galectin-8 and poly-ubiquitin and feed them into the autophagy pathway via interactions with phagophore-associated ATG8-like proteins.
Selective autophagy degrades DICER and AGO2 and regulates miRNA activity.
Voinnet et al., Zürich, Switzerland. In Nat Cell Biol, 2012
Here, we show that the miRNA-processing enzyme, DICER (also known as DICER1), and the main miRNA effector, AGO2 (also known as eukaryotic translation initiation factor 2C, 2 (EIF2C2)), are targeted for degradation as miRNA-free entities by the selective autophagy receptor NDP52 (also known as calcium binding and coiled-coil domain 2 (CALCOCO2)).
Autophagy receptors link myosin VI to autophagosomes to mediate Tom1-dependent autophagosome maturation and fusion with the lysosome.
Buss et al., Cambridge, United Kingdom. In Nat Cell Biol, 2012
Here we demonstrate that myosin VI, in concert with its adaptor proteins NDP52, optineurin, T6BP and Tom1, plays a crucial role in autophagy.
Extracellular M. tuberculosis DNA targets bacteria for autophagy by activating the host DNA-sensing pathway.
Cox et al., San Francisco, United States. In Cell, 2012
Recognition of extracelluar bacterial DNA by the STING-dependent cytosolic pathway is required for marking bacteria with ubiquitin, and delivery of bacilli to autophagosomes requires the ubiquitin-autophagy receptors p62 and NDP52 and the DNA-responsive kinase TBK1.
Regulation of Toll-like receptor signaling by NDP52-mediated selective autophagy is normally inactivated by A20.
Into et al., Gifu, Japan. In Cell Mol Life Sci, 2012
a selective autophagic mechanism mediated by NDP52 that works downstream of TRIF-TRAF6.
p62 and NDP52 proteins target intracytosolic Shigella and Listeria to different autophagy pathways.
Cossart et al., Paris, France. In J Biol Chem, 2011
p62 and NDP52 proteins target intracytosolic Shigella and Listeria to different autophagy pathways.
The ubiquitin-binding adaptor proteins p62/SQSTM1 and NDP52 are recruited independently to bacteria-associated microdomains to target Salmonella to the autophagy pathway.
Brumell et al., Toronto, Canada. In Autophagy, 2011
p62 and NDP52 act cooperatively to drive efficient antibacterial autophagy by targeting the protein complexes they coordinate to distinct microdomains associated with bacteria
Functional interaction of nuclear domain 10 and its components with cytomegalovirus after infections: cross-species host cells versus native cells.
Tang et al., Ponce, Puerto Rico. In Plos One, 2010
ND10 and ND10 components might be important defensive factors against the CMV cross-species infection
The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria.
Randow et al., Cambridge, United Kingdom. In Nat Immunol, 2009
NDP52 recognizes ubiquitin-coated Salmonella enterica and recruits TBK1.
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