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Protein kinase C and casein kinase substrate in neurons 1

H-74, PACSIN
Top mentioned proteins: Actin, Src, Dynamin I, V1a, beta 2-adrenoceptor
Papers on H-74
Cordon Bleu serves as a platform at the basal region of microvilli, where it regulates microvillar length through its WH2 domains.
Bretscher et al., Ithaca, United States. In Mol Biol Cell, 2014
Proteomic studies reveal that the COBL domain binds several BAR-containing proteins, including SNX9, PACSIN 2/syndapin 2, and ASAP1.
Syndapin--a membrane remodelling and endocytic F-BAR protein.
Review
Robinson et al., Sydney, Australia. In Febs J, 2013
Syndapin [also called PACSIN (protein kinase C and casein kinase II interacting protein)] is an Fes-CIP4 homology Bin-amphiphysin-Rvs161/167 (F-BAR) and Src-homology 3 domain-containing protein.
PICK1 interacts with PACSIN to regulate AMPA receptor internalization and cerebellar long-term depression.
Huganir et al., Baltimore, United States. In Proc Natl Acad Sci U S A, 2013
Here, we report a unique interaction between PICK1 and all three members of the protein kinase C and casein kinase II substrate in neurons (PACSIN) family and show that they form a complex with AMPARs.
Tip-to-tip interaction in the crystal packing of PACSIN 2 is important in regulating tubulation activity.
Zheng et al., Beijing, China. In Protein Cell, 2013
Here, from the crystal packing of PACSIN 2, we observed a tight tip-to-tip interaction, in addition to the wedge loop-mediated lateral interaction.
Interactions between Rab and Arf GTPases regulate endosomal phosphatidylinositol-4,5-bisphosphate during endocytic recycling.
Grant et al., Wuhan, China. In Small Gtpases, 2013
In turn this leads to over-recruitment of PI(4,5)P2-dependent membrane-bending proteins RME-1/Ehd and SDPN-1/Syndapin/PACSIN.
Casein kinase 2 phosphorylation of protein kinase C and casein kinase 2 substrate in neurons (PACSIN) 1 protein regulates neuronal spine formation.
Plomann et al., Köln, Germany. In J Biol Chem, 2013
The PACSIN (protein kinase C and casein kinase 2 substrate in neurons) adapter proteins couple components of the clathrin-mediated endocytosis machinery with regulators of actin polymerization and thereby regulate the surface expression of specific receptors.
Rigidity of wedge loop in PACSIN 3 protein is a key factor in dictating diameters of tubules.
Zheng et al., Beijing, China. In J Biol Chem, 2012
However, in the PACSIN subfamily, the F-BAR domain from PACSIN 1 and 2 can induce both high and low curvature tubules.
Identification of neuronal substrates implicates Pak5 in synaptic vesicle trafficking.
GeneRIF
Peterson et al., Philadelphia, United States. In Proc Natl Acad Sci U S A, 2012
These results implicate Pak5 in Pacsin1- and Synaptojanin1-mediated synaptic vesicle trafficking.
Phosphorylation of syndapin I F-BAR domain at two helix-capping motifs regulates membrane tubulation.
GeneRIF
Robinson et al., Sydney, Australia. In Proc Natl Acad Sci U S A, 2012
Phosphorylation of syndapin I F-BAR domain at two helix-capping motifs regulates membrane tubulation
PACSIN1 regulates the TLR7/9-mediated type I interferon response in plasmacytoid dendritic cells.
GeneRIF
Liu et al., Houston, United States. In Eur J Immunol, 2012
PACSIN1 represents a pDC-specific adaptor molecule that plays an important role in the TLR7/9-mediated type I IFN responses by pDCs in vitro and in vivo.
Cloning, purification, crystallization and preliminary X-ray diffraction analysis of mouse PACSIN 3 protein.
Zheng et al., Beijing, China. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012
PACSIN-family proteins are cytoplasmic proteins that have vesicle-transport, membrane-dynamics, actin-reorganization and microtubule activities.
Proper synaptic vesicle formation and neuronal network activity critically rely on syndapin I.
GeneRIF
Qualmann et al., Jena, Germany. In Embo J, 2012
syndapin I acts as pivotal membrane anchoring factor for dynamins during regeneration of synaptic vesicles.
PACSIN 2 represses cellular migration through direct association with cyclin D1 but not its alternate splice form cyclin D1b.
Pestell et al., Philadelphia, United States. In Cell Cycle, 2011
To investigate the mechanisms contributing to cyclin D1 functions, we purified cyclin D1a-associated complexes by affinity chromatography and identified the PACSIN 2 (protein kinase C and casein kinase substrate in neurons 2) protein by mass spectrometry.
A hinge in the distal end of the PACSIN 2 F-BAR domain may contribute to membrane-curvature sensing.
Rudolph et al., Köln, Germany. In J Mol Biol, 2010
We have obtained crystals of authentic murine PACSIN 2 that contain an ordered F-BAR domain, indicating that additional domains are flexibly connected to F-BAR.
Crystallization and preliminary X-ray crystallographic analysis of human PACSIN 1 protein.
GeneRIF
Zheng et al., Beijing, China. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2010
PACSIN 1 (1-344) was crystallized & diffracted to resolution of 3.0 A. The crystal belonged to space group C2, with unit-cell parameters a=158.65, b=87.38, c=91.76 A, alpha=90.00, beta=113.61, gamma=90.00 degrees. There are 2 molecules in asymmetric unit.
Structural requirements for PACSIN/Syndapin operation during zebrafish embryonic notochord development.
Traub et al., Cambridge, United Kingdom. In Plos One, 2008
PACSIN/Syndapin proteins are membrane-active scaffolds that participate in endocytosis.
PACSIN proteins bind tubulin and promote microtubule assembly.
GeneRIF
Plomann et al., Köln, Germany. In Exp Cell Res, 2008
These findings suggest a novel function for PACSIN proteins 1, 2, and 3 in dynamic microtubule nucleation.
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