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CLN2 Cln2p

This gene encodes a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. Mutations in this gene result in late-infantile neuronal ceroid lipofuscinosis, which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CLN3, nucleolin, PCNA, CAN, Thymopentin
Papers on CLN2
Increased expression of telomere-regulating genes in endurance athletes with long leukocyte telomeres.
Charchar et al., Armidale, Australia. In J Appl Physiol, Feb 2016
We found endurance athletes have significantly longer (7.1%, 208-416 nt) leukocyte telomeres and upregulated TERT (2.0-fold) and TPP1 (1.3-fold) mRNA expression compared with controls in age-adjusted analysis.
The Chihuahua dog: A new animal model for neuronal ceroid lipofuscinosis CLN7 disease?
Guerreiro et al., Glasgow, United Kingdom. In J Neurosci Res, Feb 2016
We studied two littermate Chihuahua dogs presenting with progressive signs of blindness, ataxia, pacing, and cognitive impairment from 1 year of age.
TPP1 Blocks an ATR-Mediated Resection Mechanism at Telomeres.
de Lange et al., New York City, United States. In Mol Cell, Feb 2016
Here we show that TPP1 and POT1a/b in shelterin block a resection pathway distinct from that repressed by TRF2.
Nucleosomes Are Essential for Proper Regulation of a Multigated Promoter in Saccharomyces cerevisiae.
Stillman et al., United States. In Genetics, Jan 2016
We modified the HO promoter with segments from the well-studied CLN2 NDR, creating chimeric promoters differing in nucleosome occupancy but with binding sites for the same activator, SBF.
Downregulation of telomerase maintenance-related ACD expression in patients undergoing immunosuppresive therapy following kidney transplantation.
Gumprecht et al., Zabrze, Poland. In Exp Ther Med, Dec 2015
Among the analyzed transcripts, the expression levels of 4 differed significantly between the studied groups; however, only the ACD (adrenocortical dysplasia homolog) gene, encoding the telomere-binding protein POT1-interacting protein 1 (TPP1), was sufficiently specific for telomere homeostasis.
The neuronal ceroid lipofuscinoses program: A translational research experience in Argentina.
Noher de Halac et al., Córdoba, Argentina. In Biochim Biophys Acta, Oct 2015
Phenotypic studies comprised epileptic seizures and movement disorders, ophthalmology, neurophysiology, image analysis, rating scales, enzyme testing, and electron microscopy, carried out under a consensus algorithm; 2) DNA screening and validation of mutations in genes PPT1 (CLN1), TPP1 (CLN2), CLN3, CLN5, CLN6, MFSD8 (CLN7), and CLN8: characterization of variant types, novel/known mutations and polymorphisms; 3) Progress of the epidemiological picture in Latin America; and 4) NCL-like pathology studies in progress.
Cell biology of the NCL proteins: What they do and don't do.
Pearce et al., Sioux Falls, United States. In Biochim Biophys Acta, Oct 2015
Some of them such as CLN1 (palmitoyl protein thioesterase 1), CLN2 (tripeptidyl-peptidase 1), CLN5, CLN10 (cathepsin D), and CLN13 (cathepsin F), are lysosomal soluble proteins; others like CLN3, CLN7, and CLN12, have been proposed to be lysosomal transmembrane proteins.
Genetics of the neuronal ceroid lipofuscinoses (Batten disease).
Cotman et al., London, United Kingdom. In Biochim Biophys Acta, Oct 2015
These genes encode lysosomal enzymes (CLN1, CLN2, CLN10, CLN13), a soluble lysosomal protein (CLN5), a protein in the secretory pathway (CLN11), two cytoplasmic proteins that also peripherally associate with membranes (CLN4, CLN14), and many transmembrane proteins with different subcellular locations (CLN3, CLN6, CLN7, CLN8, CLN12).
Shelterin proteins and cancer.
Trivedi et al., Vellore, India. In Asian Pac J Cancer Prev, 2014
It comprises six proteins, namely TRF1, TRF2, TIN2, POT1, TPP1 and RAP1.
Multiple facets of TPP1 in telomere maintenance.
Taylor et al., Cleveland, United States. In Biochim Biophys Acta, 2014
Of the primary telomere end-binding proteins, TPP1 has recently emerged as a primary contributor in protecting telomere DNA and in recruiting telomerase to the telomere ends.
Finding the end: recruitment of telomerase to telomeres.
Cech et al., Boulder, United States. In Nat Rev Mol Cell Biol, 2013
Recent work has provided insights into the mechanisms of telomerase recruitment to telomeres, highlighting the contribution of telomere-associated proteins, including TPP1 in humans, Ccq1 in Schizosaccharomyces pombe and Cdc13 and Ku70-Ku80 in Saccharomyces cerevisiae.
The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity.
Cech et al., Boulder, United States. In Nature, 2013
Shelterin includes the heterodimeric POT1-TPP1 protein, which binds the telomeric single-stranded DNA tail.
The human CST complex is a terminator of telomerase activity.
Lingner et al., Lausanne, Switzerland. In Nature, 2012
As shown in cancer cells, human telomerase binds the shelterin component TPP1 at telomeres during the S phase of the cell cycle, and adds ~60 nucleotides in a single round of extension, after which telomerase is turned off by unknown mechanisms.
TPP1 OB-fold domain controls telomere maintenance by recruiting telomerase to chromosome ends.
Artandi et al., Stanford, United States. In Cell, 2012
Study shows that the OB-fold domain of the telomere-binding protein TPP1 recruits telomerase to telomeres through an association with the telomerase reverse transcriptase TERT; data define a potential interface for telomerase-TPP1 interaction required for telomere maintenance and implicate defective telomerase recruitment in telomerase-related disease.
New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases.
Oda, Kyoto, Japan. In J Biochem, 2012
Studies indicate that TPP-I is the only member of the sedolisin family that has been shown to exhibit tripeptidyl peptidase activity and is related to the fatal hereditary disease, Batten disease.
Yeast IME2 functions early in meiosis upstream of cell cycle-regulated SBF and MBF targets.
Sawarynski et al., Detroit, United States. In Plos One, 2011
Ime2 does not directly catalyze Sic1 phosphorylation to target it for destabilization as Cln1,-2/Cdk1 do during the cell cycle
Telomere protection by TPP1/POT1 requires tethering to TIN2.
de Lange et al., New York City, United States. In Mol Cell, 2011
Telomere protection by TPP1/POT1 requires tethering to TIN2.
Developmental study of tripeptidyl peptidase I activity in the mouse central nervous system and peripheral organs.
Ivanov et al., Sofia, Bulgaria. In Cell Tissue Res, 2011
TPPI activity becomes crucial for the neuronal functions later in development.
TERRA and hnRNPA1 orchestrate an RPA-to-POT1 switch on telomeric single-stranded DNA.
Zou et al., United States. In Nature, 2011
These two processes use two single-stranded DNA (ssDNA)-binding proteins, replication protein A (RPA) and protection of telomeres 1 (POT1).
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