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ADAMTS-like 1

punctin, punctin-1, ADAMTS-like, ADAMTSL-1, ADAMTSL, ADAMTS-like 1
This gene encodes a secreted protein and member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) family. This protein lacks the metalloproteinase and disintegrin-like domains, which are typical of the ADAMTS family, but contains other ADAMTS domains, including the thrombospondin type 1 motif. This protein may have important functions in the extracellular matrix. Alternative splicing results in multiple transcript variants encoding distinct proteins. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ADAMTS, thrombospondin-1, fibrillin-1, CD45, metalloprotease
Papers on punctin
Disruption of murine Adamtsl4 results in zonular fiber detachment from the lens and in retinal pigment epithelium dedifferentiation.
Nishina et al., Bar Harbor, United States. In Hum Mol Genet, Jan 2016
Mutations in human ADAMTSL4, encoding an ADAMTS-like protein which has been implicated in fibrillin microfibril biogenesis, cause ectopia lentis (EL) and EL et pupillae.
Melanocyte antigen triggers autoimmunity in human psoriasis.
Prinz et al., München, Germany. In J Exp Med, Jan 2016
Through peptide library screening, we identified ADAMTS-like protein 5 (ADAMTSL5) as an HLA-C*06:02-presented melanocytic autoantigen of the Vα3S1/Vβ13S1 TCR.
ADAMTS proteins as modulators of microfibril formation and function.
Apte et al., Cleveland, United States. In Matrix Biol, Sep 2015
The ADAMTS (a disintegrin-like and metalloproteinase domain with thrombospondin-type 1 motifs) protein superfamily includes 19 secreted metalloproteases and 7 secreted ADAMTS-like (ADAMTSL) glycoproteins.
MADD-4/Punctin and Neurexin Organize C. elegans GABAergic Postsynapses through Neuroligin.
Shen et al., Stanford, United States. In Neuron, Jul 2015
Two presynaptic factors, Punctin/MADD-4, an ADAMTS-like extracellular protein, and neurexin/NRX-1, act partially redundantly to recruit NLG-1 to synapses.
Transcriptional coordination of synaptogenesis and neurotransmitter signaling.
Hobert et al., New York City, United States. In Curr Biol, Jun 2015
UNC-3 directly controls the expression of the ADAMTS-like protein MADD-4/Punctin, a presynaptically secreted synapse-organizing molecule that clusters postsynaptic receptors.
Insights on ADAMTS proteases and ADAMTS-like proteins from mammalian genetics.
Apte et al., Cleveland, United States. In Matrix Biol, May 2015
The mammalian ADAMTS superfamily comprises 19 secreted metalloproteinases and 7 ADAMTS-like proteins, each the product of a distinct gene.
EVA-1 functions as an UNC-40 Co-receptor to enhance attraction to the MADD-4 guidance cue in Caenorhabditis elegans.
Roy et al., Toronto, Canada. In Plos Genet, 2014
We recently discovered a secreted and diffusible midline cue called MADD-4 (an ADAMTSL) that guides migrations along the dorsoventral axis of the nematode Caenorhabditis elegans.
Glia ECM interactions are required to shape the Drosophila nervous system.
Klämbt et al., Münster, Germany. In Mech Dev, 2014
To identify further components controlling nervous system shape we performed an RNAi based screen and identified the gene nolo, which encodes an ADAMTS-like protein.
C. elegans Punctin specifies cholinergic versus GABAergic identity of postsynaptic domains.
Bessereau et al., France. In Nature, 2014
5), the C. elegans orthologue of mammalian punctin-1 and punctin-2, encodes neurally secreted isoforms that specify the excitatory or inhibitory identity of postsynaptic NMJ domains.
Matricellular proteins in development: perspectives from the Drosophila heart.
Paululat et al., Israel. In Matrix Biol, 2014
Loh is an ADAMTS-like protein, which serves as an adapter protein to Pericardin (a collagen-like protein), promoting its specific localization at the abluminal domain of the heart tube.
Time-resolved analysis of the matrix metalloproteinase 10 substrate degradome.
auf dem Keller et al., Zürich, Switzerland. In Mol Cell Proteomics, 2014
By applying this strategy to dissect the matrix metalloproteinase 10 (MMP10) substrate degradome in fibroblast secretomes, we identified the extracellular matrix protein ADAMTS-like protein 1 (ADAMTSL1) as a direct MMP10 substrate and revealed MMP10-dependent ectodomain shedding of platelet-derived growth factor receptor alpha (PDGFRα) as well as sequential processing of type I collagen.
The conserved ADAMTS-like protein lonely heart mediates matrix formation and cardiac tissue integrity.
Paululat et al., Osnabrück, Germany. In Plos Genet, 2012
Here we report on the identification and functional characterization of the ADAMTS-like homolog lonely heart (loh) in Drosophila melanogaster.
A disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (ADAMTS) superfamily: functions and mechanisms.
Apte, Cleveland, United States. In J Biol Chem, 2009
Together with seven ADAMTS-like proteins, the 19 mammalian ADAMTS proteases constitute a superfamily.
Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.
Apte et al., Cleveland, United States. In J Biol Chem, 2009
thrombospondin type-1 repeats from punctin-1 carries C-mannosylation in close proximity to O-linked fucose
Peters'-plus syndrome is a congenital disorder of glycosylation caused by a defect in the beta1,3-glucosyltransferase that modifies thrombospondin type 1 repeats.
Maki et al., Tampere, Finland. In Ann Med, 2008
Some ninety human proteins contain TSRs, but thus far the disaccharide has been demonstrated on only thrombospondin 1, properdin, F-spondin, ADAMTS-13, and ADAMTSL-1.
ADAMTSL2 mutations in geleophysic dysplasia demonstrate a role for ADAMTS-like proteins in TGF-beta bioavailability regulation.
Cormier-Daire et al., Paris, France. In Nat Genet, 2008
Geleophysic dysplasia is an autosomal recessive disorder characterized by short stature, brachydactyly, thick skin and cardiac valvular anomalies often responsible for an early death.
O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily.
Apte et al., Cleveland, United States. In J Biol Chem, 2007
data define a critical role for N-glycosylation and O-fucosylation in the biosynthesis of punctin-1
Punctin, a novel ADAMTS-like molecule, ADAMTSL-1, in extracellular matrix.
Apte et al., Cleveland, United States. In J Biol Chem, 2002
Punctin, a novel ADAMTS-like molecule, ADAMTSL-1, in extracellular matrix
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