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Protein kinase C and casein kinase substrate in neurons 2

PACSIN 2, syndapin II
This gene is a member of the protein kinase C and casein kinase substrate in neurons family. The encoded protein is involved in linking the actin cytoskeleton with vesicle formation by regulating tubulin polymerization. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2010] (from NCBI)
Top mentioned proteins: H-74, beta 2-adrenoceptor, Actin, Dynamin I, CAN
Papers on PACSIN 2
Possible regulation of caveolar endocytosis and flattening by phosphorylation of F-BAR domain protein PACSIN2/Syndapin II.
Suetsugu et al., Helsinki, Finland. In Bioarchitecture, Feb 2016
PACSIN2/Syndapin II is one of the BAR domain-containing proteins, and is localized at the necks of caveolae.
OCRL1 engages with the F-BAR protein pacsin 2 to promote biogenesis of membrane-trafficking intermediates.
Lowe et al., Manchester, United Kingdom. In Mol Biol Cell, Feb 2016
OCRL1 interacts via IPIP27A with the F-BAR protein pacsin 2. OCRL1 and IPIP27A localize to mannose 6-phosphate receptor (MPR)-containing trafficking intermediates, and loss of either protein leads to defective MPR carrier biogenesis at the TGN and endosomes.
Phosphorylation of PACSIN2 by protein kinase C triggers the removal of caveolae from the plasma membrane.
Suetsugu et al., Tokyo, Japan. In J Cell Sci, Sep 2015
PACSIN2, a membrane-sculpting BAR domain protein, localizes to caveolae.
FlnA binding to PACSIN2 F-BAR domain regulates membrane tubulation in megakaryocytes and platelets.
Falet et al., Boston, United States. In Blood, Aug 2015
The F-BAR protein PACSIN2 is one of the most abundant BAR/F-BAR proteins in platelets and the only one reported to interact with the cytoskeletal and scaffold protein filamin A (FlnA), an essential regulator of platelet formation and function.
Myocardin Family Members Drive Formation of Caveolae.
Swärd et al., Lund, Sweden. In Plos One, 2014
PACSIN2 also increased, establishing positive regulation of caveolae genes from three families.
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.
Cerebellar transcriptional alterations with Purkinje cell dysfunction and loss in mice lacking PGC-1α.
Cowell et al., Birmingham, United States. In Front Cell Neurosci, 2013
We found significant reductions in transcripts with synaptic (complexin1, Cplx1; Pacsin2), structural (neurofilament heavy chain, Nefh), and metabolic (isocitrate dehydrogenase 3a, Idh3a; neutral cholesterol ester hydrolase 1, Nceh1; pyruvate dehydrogenase alpha 1, Pdha1; phytanoyl-CoA hydroxylase, Phyh; ubiquinol-cytochrome c reductase, Rieske iron-sulfur polypeptide 1, Uqcrfs1) functions.
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
Similarly, the binding of PICK1 to the ubiquitously expressed PACSIN2 is also regulated by the homologous phosphorylation sites within the PACSIN2-variable region.
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.
Physicochemical analysis from real-time imaging of liposome tubulation reveals the characteristics of individual F-BAR domain proteins.
Takiguchi et al., Nagoya, Japan. In Langmuir, 2013
Here, we successfully monitored the entire process of tubulation and the behavior of elongated tubules caused by four different F-BAR domain family proteins (FBP17, CIP4, PSTPIP1, and Pacsin2) using direct real-time imaging of giant unilamellar liposomes with dark-field optical microscopy.
The F-BAR protein PACSIN2 regulates epidermal growth factor receptor internalization.
Hordijk et al., Amsterdam, Netherlands. In J Biol Chem, 2013
In this study, we identify a novel role for the F-BAR protein PACSIN2 in the regulation of EGF receptor signaling.
Molecular composition and ultrastructure of the caveolar coat complex.
Nichols et al., Cambridge, United Kingdom. In Plos Biol, 2012
Caveolin and cavin proteins, as well as EHD2 and pacsin 2, are all present in caveolae.
Nucleophosmin1 is a negative regulator of the small GTPase Rac1.
Hordijk et al., Amsterdam, Netherlands. In Plos One, 2012
We have previously identified several effector proteins of Rac1 that also act as Rac1 regulatory proteins, including caveolin-1 and PACSIN2.
Multilocus genotypes of relevance for drug metabolizing enzymes and therapy with thiopurines in patients with acute lymphoblastic leukemia.
Decorti et al., Memphis, United States. In Front Genet, 2011
The use of high-throughput genomic analysis allows identification of additional candidate genetic factors associated with pharmacogenetic phenotypes, such as TPMT enzymatic activity: PACSIN2 polymorphisms have been identified by a genome-wide analysis, combining evaluation of polymorphisms and gene expression, as a significant determinant of TPMT activity in the HapMap CEU cell lines and the effects of PACSIN2 on TPMT activity and mercaptopurine induced adverse effects were confirmed in children with ALL.
Pacsin 2 is recruited to caveolae and functions in caveolar biogenesis.
Nichols et al., Cambridge, United Kingdom. In J Cell Sci, 2011
important role in the formation of plasma membrane caveolae
The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell spreading and migration.
Hordijk et al., Amsterdam, Netherlands. In J Cell Sci, 2011
Data identify the BAR-domain protein PACSIN2 as a Rac1 interactor that regulates Rac1-mediated cell spreading and migration.
Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting.
Suetsugu et al., Tokyo, Japan. In J Cell Sci, 2011
Results indicate that PACSIN2 mediates membrane sculpting by caveolin-1 in caveola morphology and recruits dynamin-2 for caveola fission.
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
PACSIN2 regulates cell spreading and cell migration, which are dependent on cyclin D1 expression.
Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II.
Suetsugu et al., Yokohama, Japan. In Febs Lett, 2010
Since the curvature of the neck of the microspike and that of the tubulation share similar geometry, the pacsin2 EFC/F-BAR domain is considered to facilitate both microspike formation and tubulation.
Dietary Supplementation of Vitamin E and α-Lipoic Acid Upregulates Cell Growth and Signaling Genes in Rat Myocardium.
Coombes et al., Brisbane, Australia. In Int J Biomed Sci, 2006
Upregulated genes include those involved in cell growth and maintenance (LynB, Csf1r, Akt2, Tp53), cell signaling (LynB, Csf1r) and signal transduction (Pacsin2, Csf1r).
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