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

ArfGAP with coiled-coil, ankyrin repeat and PH domains 1

ACAP1, CENTB1, Centaurin beta1
Top mentioned proteins: ARF6, GAP, p16, CAN, ARF1
Papers on ACAP1
An ACAP1 coat complex acting in endocytic recycling.
Hsu et al., Boston, United States. In Methods Cell Biol, 2014
Leading this charge have been studies on a coat complex defined by ACAP1 (adenosine diphosphate ribosylation factor GTPase-activating proteins with Coiled-coil, Ankryin repeat and PH domains 1), which acts in the sorting of cargoes at the recycling endosome for their return to the plasma membrane.
The Arf GTPase-activating protein family is exploited by Salmonella enterica serovar Typhimurium to invade nonphagocytic host cells.
Koronakis et al., Cambridge, United Kingdom. In Mbio, 2014
The Arf6 GAPs ACAP1 and ADAP1 and the Arf1 GAP ASAP1 localized at Salmonella-induced ruffles, which was not the case for the plasma membrane-localized Arf6 GAPs ARAP3 and GIT1 or the Golgi-associated Arf1 GAP1.
Translational study of Alzheimer's disease (AD) biomarkers from brain tissues in AβPP/PS1 mice and serum of AD patients.
Wang et al., Beijing, China. In J Alzheimers Dis, 2014
Of these 11 proteins, levels of 5 changed in the same direction in the serum of AD patients as they did in mouse brain: cathepsin B, VDAC1, and cofilin-2 increased, and Alix and ACAP1 decreased.
The Arf6 GTPase-activating proteins ARAP2 and ACAP1 define distinct endosomal compartments that regulate integrin α5β1 traffic.
Randazzo et al., Bethesda, United States. In J Biol Chem, 2014
Arf6 and the Arf6 GTPase-activating protein (GAP) ACAP1 are established regulators of integrin traffic important to cell adhesion and migration.
A PH domain in ACAP1 possesses key features of the BAR domain in promoting membrane curvature.
Sun et al., Beijing, China. In Dev Cell, 2014
ACAP1 (Arfgap with Coil coil, Ankyrin repeat, and PH domain protein 1) contains a BAR domain.
A novel twist in membrane dePHormation.
Haucke et al., Berlin, Germany. In Dev Cell, 2014
(2014) show that the BAR domain of ACAP1, although architecturally similar to other BAR domains, cooperates with its neighboring pleckstrin homology domain to deform membranes and facilitate endosomal recycling.
Arf1 and Arf6 promote ventral actin structures formed by acute activation of protein kinase C and Src.
Donaldson et al., Bethesda, United States. In Cytoskeleton (hoboken), 2014
Furthermore, expression of ASAP1, an Arf1 GTPase activating protein (GAP) was more effective at inhibiting the ventral actin structures than was ACAP1, an Arf6 GAP.
ZRANB2 localizes to supraspliceosomes and influences the alternative splicing of multiple genes in the transcriptome.
Morris et al., Sydney, Australia. In Mol Biol Rep, 2013
At the FDR ≤1.3 significance level we found that ZRANB2 influenced the alternative splicing of primary transcripts of CENTB1, WDR78, C10orf18, CABP4, SMARCC2, SPATA13, OR4C6, ZNF263, CAPN10, SALL1, ST18 and ZP2.
Pattern-recognition receptor signaling regulator mRNA expression in humans and mice, and in transient inflammation or progressive fibrosis.
Lech et al., München, Germany. In Int J Mol Sci, 2012
We therefore determined the mRNA expression levels of A20, CYLD, DUBA, ST2, CD180, SIGIRR, TANK, SOCS1, SOCS3, SHIP, IRAK-M, DOK1, DOK2, SHP1, SHP2, TOLLIP, IRF4, SIKE, NLRX1, ERBIN, CENTB1, and Clec4a2 in human and mouse solid organs.
RAB-10-GTPase-mediated regulation of endosomal phosphatidylinositol-4,5-bisphosphate.
Grant et al., United States. In Proc Natl Acad Sci U S A, 2012
One RAB-10-binding partner that we identified, CNT-1, is the only C. elegans homolog of the mammalian Arf6 GTPase-activating proteins ACAP1 and ACAP2.
Mechanistic insights into regulated cargo binding by ACAP1 protein.
Hsu et al., Boston, United States. In J Biol Chem, 2012
phosphorylation of ACAP1 relieves a localized mechanism of autoinhibition in regulating cargo binding
ARF6 directs axon transport and traffic of integrins and regulates axon growth in adult DRG neurons.
Fawcett et al., Cambridge, United Kingdom. In J Neurosci, 2012
ARF6 inactivation by expression of ACAP1 leads to increased recycling of β1 integrins to the neuronal surface and to increased anterograde axonal transport.
Somatic mutations in the Notch, NF-KB, PIK3CA, and Hedgehog pathways in human breast cancers.
Sjöblom et al., Uppsala, Sweden. In Genes Chromosomes Cancer, 2012
Somatic mutations with potential impact on protein function were observed in the genes ADAM12, CENTB1, CENTG1, DIP2C, GLI1, GRIN2D, HDLBP, IKBKB, KPNA5, NFKB1, NOTCH1, and OTOF.
The oncogenic TBC domain protein USP6/TRE17 regulates cell migration and cytokinesis.
Haucke et al., Berlin, Germany. In Biol Cell, 2012
the oncogenic potential of USP6 is linked to its ability to integrate cell migration and cytokinesis by regulating Arf6/ACAP1.
Biogenesis and regulation of insulin-responsive vesicles containing GLUT4.
Kandror et al., New Haven, United States. In Curr Opin Cell Biol, 2010
Formation of the insulin-responsive vesicles requires multiple interactions among GLUT4, IRAP, LRP1, and sortilin, as well as recruitment of GGA and ACAP1 adaptors and clathrin.
Substrate specificities and activities of AZAP family Arf GAPs in vivo.
Casanova et al., Charlottesville, United States. In Am J Physiol Cell Physiol, 2008
ACAP1 has robust, constitutive Arf6 GAP activity in vivo, with little activity toward Arf1.
An ACAP1-containing clathrin coat complex for endocytic recycling.
Hsu et al., Boston, United States. In J Cell Biol, 2007
Results suggest that ACAP1, a GTPase-activating protein (GAP) for ADP-ribosylation factor (ARF) 6, is part of a novel clathrin coat complex that is regulated by ARF6 for endocytic recycling in two key physiological settings.
Cooperation of phosphoinositides and BAR domain proteins in endosomal tubulation.
Shibasaki et al., Tokyo, Japan. In Traffic, 2006
Results suggest that two ARF6 downstream molecules, PIP5K and ACAP1, function together in endosomal tubulation and that phosphoinositide levels may regulate endosomal dynamics.
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