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CutA divalent cation tolerance homolog

CutA, AtCutA, protein cutA
may play a role in anchoring acetylcholinesterase in neuronal cell membranes; may be involved in signal transduction [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: acetylcholinesterase, CAN, ACID, V1a, 20-kDa
Papers on CutA
[Identification of proteins interacting with the circadian clock protein PER1 in tumors using bacterial two-hybrid system technique].
Ma et al., Chengdu, China. In Zhonghua Yi Xue Yi Chuan Xue Za Zhi, Apr 2015
RESULTS: Fourteen protein coding genes were identified, 4 of which were found to contain whole coding regions of genes, which included optic atrophy 3 protein (OPA3) associated with mitochondrial dynamics and homo sapiens cutA divalent cation tolerance homolog of E. coli (CUTA) associated with copper metabolism.
Role of copper and the copper-related protein CUTA in mediating APP processing and Aβ generation.
Zhang et al., Xiamen, China. In Neurobiol Aging, Mar 2015
Recently, we find that a copper-related protein, CutA divalent cation tolerance homolog of Escherichia coli (CUTA), interacts with the β-secretase β-site APP cleaving enzyme 1 (BACE1) and inhibits APP β-processing and Aβ generation.
The gene cutA of Fusarium fujikuroi, encoding a protein of the haloacid dehalogenase family, is involved in osmotic stress and glycerol metabolism.
Avalos et al., Sevilla, Spain. In Microbiology, 2014
Here we report on the functional analysis of cutA, the orthologous gene in the phytopathogenic fungus Fusarium fujikuroi.
Two-component protein hydrogels assembled using an engineered disulfide-forming protein-ligand pair.
Chen et al., College Station, United States. In Biomacromolecules, 2013
The building blocks of the hydrogel are two liquid-phase protein block copolymers each containing (1) a subunit of the trimeric protein CutA as a cross-linker and (2) one member of a PDZ-domain-containing protein-ligand pair whose interaction was reinforced by an engineered disulfide linkage.
CutA divalent cation tolerance homolog (Escherichia coli) (CUTA) regulates β-cleavage of β-amyloid precursor protein (APP) through interacting with β-site APP cleaving protein 1 (BACE1).
Zhang et al., Xiamen, China. In J Biol Chem, 2012
H component of CUTA as a novel BACE1-interacting protein that mediates the intracellular trafficking of BACE1 and the processing of APP to Abeta
Microarray and proteomic analysis of breast cancer cell and osteoblast co-cultures: role of osteoblast matrix metalloproteinase (MMP)-13 in bone metastasis.
Overall et al., Vancouver, Canada. In J Biol Chem, 2011
These included inactivation of the chemokines CCL2 and CCL7, activation of platelet-derived growth factor-C, and cleavage of SAA3, osteoprotegerin, CutA, and antithrombin III.
Distinct roles for Caf1, Ccr4, Edc3 and CutA in the co-ordination of transcript deadenylation, decapping and P-body formation in Aspergillus nidulans.
Caddick et al., Liverpool, United Kingdom. In Mol Microbiol, 2010
P-body formation is disrupted in A. nidulans strains deleted for Edc3, an enhancer of decapping, or CutA, which encodes a nucleotidyltransferase that triggers mRNA decapping by the addition of a CUCU tag to the poly(A) tail.
Reversible hydrogel formation driven by protein-peptide-specific interaction and chondrocyte entrapment.
Matsuda et al., Kawaguchi, Japan. In Biomaterials, 2010
We developed a hydrogel self-assembling method driven by the interaction between recombinant tax-interactive protein-1 (TIP1) with the PDZ domain in a molecule, which is fused to each end of the triangular trimeric CutA protein (CutA-TIP1), and a PDZ domain-recognizable peptide which is covalently bound to each terminus of four-armed poly(ethylene glycol) (PDZ-peptide-PEG).
Involvement of N-acetyltransferase human in the cytotoxic activity of 5-fluorouracil.
Shiota et al., Yonago, Japan. In Anticancer Drugs, 2009
Profilin 1, CutA, ras-related nuclear protein, annexin A5, enolase 1, and elongation factor 1 alpha 1 were found to be upregulated and 14-3-3eta, tublin, nuclear auto antigenic sperm protein, heat shock protein 70, and heat shock protein 90 were downregulated by knockdown of NATH.
Unusual transfer of CutA into the secretory pathway, evidenced by fusion proteins with acetylcholinesterase.
Massoulié et al., Paris, France. In Febs J, 2009
an N-terminal CutA domain actually drives AChE into the endoplasmic reticulum and allows its secretion
Protein CutA undergoes an unusual transfer into the secretory pathway and affects the folding, oligomerization, and secretion of acetylcholinesterase.
Massoulié et al., Paris, France. In J Biol Chem, 2009
Protein CutA undergoes an unusual transfer into the secretory pathway and affects the folding, oligomerization, and secretion of acetylcholinesterase.
Characterization of the human CUTA isoform2 present in the stably transfected HeLa cells.
Yu et al., Shanghai, China. In Mol Biol Rep, 2009
expression profile of CUTA gene in tissues was examined & revealed CUTA gene was constitutively expressed in the 18 tissues tested; CUTA isoform2 was mainly located in mitochondria as a new potential mitochondrial protein
Overexpression of human CUTA isoform2 enhances the cytotoxicity of copper to HeLa cells.
Yu et al., Shanghai, China. In Acta Biochim Pol, 2007
Human CUTA isoform2 is a member of cation tolerance protein (CutA1) family.
The 2.2 A resolution crystal structure of Bacillus cereus Nif3-family protein YqfO reveals a conserved dimetal-binding motif and a regulatory domain.
Anderson et al., Portland, United States. In Protein Sci, 2007
It also reveals the previously unknown structure of the insert, which despite extremely limited sequence conservation, bears great similarity to PII, CutA, and a number of other trimeric regulatory proteins.
Structural evidence for guanidine-protein side chain interactions: crystal structure of CutA from Pyrococcus horikoshii in 3 M guanidine hydrochloride.
Kumagai et al., Sendai, Japan. In Biochem Biophys Res Commun, 2004
Crystal structure of CutA from an archaeon Pyrococcus horikosii (PhoCutA), a heavy-metal binding protein, was determined at 1.6-angstroms resolution in the presence of 3 M guanidine HCl (GdnHCl).
The evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transduction.
Viezzoli et al., Sesto Fiorentino, Italy. In J Biol Chem, 2003
comparative x-ray crystallography analysis suggests CutA1 proteins have a role in signal transduction through allosteric communications between subunits.
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