Yuichi Mazaki

ORCID: 0000-0003-4192-0834
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About
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Research Areas
  • Cell Adhesion Molecules Research
  • Nitric Oxide and Endothelin Effects
  • S100 Proteins and Annexins
  • Receptor Mechanisms and Signaling
  • Cellular transport and secretion
  • Neutrophil, Myeloperoxidase and Oxidative Mechanisms
  • Protein Kinase Regulation and GTPase Signaling
  • Ion channel regulation and function
  • Cellular Mechanics and Interactions
  • Ferroptosis and cancer prognosis
  • Mitochondrial Function and Pathology
  • RNA modifications and cancer
  • Genomics, phytochemicals, and oxidative stress
  • Monoclonal and Polyclonal Antibodies Research
  • Ubiquitin and proteasome pathways
  • Protease and Inhibitor Mechanisms
  • Free Radicals and Antioxidants
  • Redox biology and oxidative stress
  • Adipose Tissue and Metabolism
  • Endoplasmic Reticulum Stress and Disease
  • Advanced Glycation End Products research
  • Phytochemicals and Antioxidant Activities
  • ATP Synthase and ATPases Research
  • Parkinson's Disease Mechanisms and Treatments
  • Pulmonary Hypertension Research and Treatments

Hokkaido University
2016-2025

Pharmac
2019-2022

Kumamoto University
2012

Osaka University
1998-2007

Osaka Science Museum
2004

Kyoto University
1997-1998

National Institute for Basic Biology
1996-1998

Integrins can intercommunicate with cadherins. Here, we examined their possible relationship by use of small interfering RNA–mediated protein knockdown in HeLa cells. We found that a subset integrin signaling molecules, namely Fak and paxillin, but not p130 Crk-associated substrate or proline-rich tyrosine kinase 2, participate processes regulating N-cadherin–based cell–cell adhesion. Paxillin was to be required primarily for the recruitment robust focal adhesions. Our results suggest at...

10.1083/jcb.200312013 article EN The Journal of Cell Biology 2004-07-19

RhoA activity is transiently inhibited at the initial phase of integrin engagement, when Cdc42- and/or Rac1-mediated membrane spreading and ruffling predominantly occur. Paxillin, an integrin-assembly protein, has four major tyrosine phosphorylation sites, Tyr31 Tyr118 correlates with cell adhesion migration. We found that mutation Tyr31/118 caused enhanced activation premature formation stress fibers substantial loss efficient in migration NMuMG cells. These phenotypes were similar to those...

10.1083/jcb.200202117 article EN The Journal of Cell Biology 2002-11-25

Mitfencodes a basic helix-loop-helix-leucine-zipper (bHLHzip) protein that is known to function in the development of melanocytes, pigmented epithelial cells (PECs), osteoclasts, and mast cells. In this paper, we report on isolation, expression, overexpression chickenMitfand discuss role its product differentiation transdifferentiation PECs. Northern blotting showed chickenMitfis predominantly expressed embryonic retinal epithelium (PE), but at low levels other tissues. A 5′ RACE analysis...

10.1006/dbio.1997.8800 article EN cc-by-nc-nd Developmental Biology 1998-01-01

Paxillin acts as an adaptor molecule in integrin signaling. is localized to focal contacts but seems also exist a relatively large cytoplasmic pool. Here, we report the identification of new paxillin-binding protein, PAG3 (paxillin-associated protein with ADP-ribosylation factor [ARF] GTPase-activating [GAP] activity, number 3), which involved regulation subcellular localization paxillin. bound all paxillin isoforms and was induced during monocyte maturation, at time expression increased...

10.1091/mbc.11.4.1315 article EN Molecular Biology of the Cell 2000-04-01

Using mass spectrometry we have identified proteins which co-immunoprecipitate with paxillin, an adaptor protein implicated in the integrin-mediated signaling pathways of cell motility. A major component paxillin immunoprecipitates was poly(A)-binding 1, a 70-kDa mRNA-binding protein. Poly(A)-binding 1 associated both α and β isoforms this unaffected by RNase treatment consistent protein-protein interaction. The NH<sub>2</sub>-terminal region (residues 54–313) directly lysates,...

10.1074/jbc.m109446200 article EN cc-by Journal of Biological Chemistry 2002-02-01

Paxillin acts as an adaptor protein in integrin signaling. We have shown that paxillin exists a relatively large cytoplasmic pool, including perinuclear areas, addition to focal complexes formed at the cell periphery and adhesions underneath cell. Several ADP-ribosylation factor (ARF) GTPase-activating proteins (GAPs; ARFGAPs) been associate with paxillin. report here Git2-short/KIAA0148 exhibits properties of paxillin-associated ARFGAP appears be colocalized paxillin, primarily areas. A...

10.1091/mbc.12.3.645 article EN Molecular Biology of the Cell 2001-03-01

Most chemoattractants for neutrophils bind to the Gα i family of heterotrimeric G protein–coupled receptors (GPCRs) and release Gβγ subunits activate chemotaxis superoxide production. GIT2, a GTPase-activating protein Arf1, forms complex with is integral directional sensing suppression Here we show that GBF1, guanine nucleotide exchanging factor Arf-GTPases, primarily responsible Arf1 activation upon GPCR stimulation important neutrophil We find GBF1 bears novel module, namely binding...

10.1091/mbc.e12-01-0062 article EN cc-by-nc-sa Molecular Biology of the Cell 2012-05-10

Background Accumulating evidence has shown that methionine- and choline-deficient high fat (MCD+HF) diet induces the development of nonalcoholic fatty liver disease (NAFLD), in which elevated reactive oxygen species play a crucial role. We have reported peroxiredoxin 4 (PRDX4), unique secretory member PRDX antioxidant family, protects against NAFLD progression. However, detailed mechanism potential effects on intestinal function still remain unclear. Methods & Results Two weeks after feeding...

10.1371/journal.pone.0152549 article EN cc-by PLoS ONE 2016-04-01

The versatility of integrin functions is mediated by engagement a number proteins that assemble with integrins. Among them, paxillin one the important molecules interacting variety signaling and cytoskeletal building blocks. We report here not single molecule unique physiological property. identified two human isoforms, β γ. These isoforms have distinct amino acid insertions; each consists exon, at same site previously reported (paxillin α). Several were co-precipitated paxillin, we found...

10.1074/jbc.272.11.7437 article EN cc-by Journal of Biological Chemistry 1997-03-01

p21-activated kinases (PAKs) are implicated in integrin signalings, and have been proposed to associate with paxillin indirectly. We show here that can bind directly PAK3. examined several representative focal adhesion proteins, found is the sole protein associates PAK3 associated alpha beta isoforms of paxillin, but not gamma. also both kinase-inactive Cdc42-activated forms vivo, without affecting activation states kinase. A number different functions ascribed PAKs; PAKs growth factor...

10.1074/jbc.m005854200 article EN cc-by Journal of Biological Chemistry 2001-02-01

The Fcγ receptor (FcγR)-mediated phagocytosis of macrophages is a complex process where remodeling both the actin-based cytoskeleton and plasma membrane occur coordinately. Several different families small GTPases are involved. We have isolated GTPase-activating protein (GAP) for ADP-ribosylation factor (ARF), paxillin-associated with ARFGAP activity (PAG)3/Papα/KIAA0400, from mature monocytes macrophage-like cells. Mammalian ARFs fall into three classes, class III isoform (ARF6) has been...

10.1084/jem.193.8.955 article EN The Journal of Experimental Medicine 2001-04-16

Paxillin, a focal adhesion protein, exists as multiple isoforms in humans (α, β, and γ). To understand more about the physiological role of each isoform, we have employed mouse system. We found that although α β are present mouse, γ isoform is not. The protein was detected clearly most adult tissues, whereas almost undetectable except spleen, testis, thymus, lung. On other hand, mRNAs both were detectable all tissues examined. High levels peritoneal exudate macrophage cells well cultured...

10.1074/jbc.273.35.22435 article EN cc-by Journal of Biological Chemistry 1998-08-01

Endothelin-1 (ET-1) reduces insulin-stimulated glucose uptake in skeletal muscle, inducing insulin resistance. Here, we have determined the molecular mechanisms underlying negative regulation by ET-1 of signalling.We used rat L6 muscle cells fully differentiated into myotubes. Changes phosphorylation Akt was assessed Western blotting. Effects on with [(3) H]-2-deoxy-d-glucose ([(3) H]2-DG). The C-terminus region GPCR kinase 2 (GRK2-ct), a dominant GRK2, overexpressed using...

10.1111/bph.13406 article EN British Journal of Pharmacology 2015-12-11

The small GTP-binding protein Arf6 regulates membrane remodeling at cell peripheries and plays crucial roles in higher orders of cellular functions including tumor invasion. Here we show that Fbx8, an F-box bearing the Sec7 domain, mediates ubiquitination Arf6. This did not appear to be linked immediate proteasomal degradation Arf6, whereas Fbx8 knockdown caused hyperactivation Expression was substantially lost several breast lines, which activity is pivotal for their Forced expression these...

10.1091/mbc.e07-08-0763 article EN Molecular Biology of the Cell 2007-12-20

Neutrophils depend heavily on glycolysis for energy production under normal conditions. In contrast, neutrophils require supplied by mitochondrial oxidative phosphorylation (OXPHOS) during chemotaxis. However, the mechanism which supply changes from to OXPHOS remains unknown. Leucine-rich repeat kinase 2 (LRRK2) is partially present in outer membrane fraction. Lrrk2-deficient cells show fragmentation and reduced activity. We have previously reported that mitofusin (MFN) involved chemotaxis...

10.1186/s12964-023-01305-y article EN cc-by Cell Communication and Signaling 2023-10-30
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