Phosphorylation of Kindlins and the Control of Integrin Function
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Myosin Myth4-FERM Structures Highlight Important Principles of Convergent Evolution
Myosin MyTH4-FERM structures highlight important principles of convergent evolution Vicente José Planelles-Herreroa,b, Florian Blanca,c, Serena Sirigua, Helena Sirkiaa, Jeffrey Clausea, Yannick Souriguesa, Daniel O. Johnsrudd, Beatrice Amiguesa, Marco Cecchinic, Susan P. Gilberte, Anne Houdussea,1,2, and Margaret A. Titusd,1,2 aStructural Motility, Institut Curie, CNRS, UMR 144, PSL Research University, F-75005 Paris, France; bUPMC Université de Paris 6, Institut de Formation Doctorale, Sorbonne Universités, 75252 Paris Cedex 05, France; cLaboratoire d’Ingénierie des Fonctions Moléculaires, Institut de Science et d’Ingénierie Supramoléculaires, UMR 7006 CNRS, Université de Strasbourg, F-67083 Strasbourg Cedex, France; dDepartment of Genetics, Cell Biology and Development, University of Minnesota, Minneapolis, MN 55455; and eDepartment of Biological Sciences, Rensselaer Polytechnic Institute, Troy, NY 12180 Edited by James A. Spudich, Stanford University School of Medicine, Stanford, CA, and approved March 31, 2016 (received for review January 15, 2016) Myosins containing MyTH4-FERM (myosin tail homology 4-band (Fig. 1). These MF myosins are widespread and likely quite an- 4.1, ezrin, radixin, moesin, or MF) domains in their tails are found cient because they are found in many different branches of the in a wide range of phylogenetically divergent organisms, such as phylogenetic tree (5, 6), including Opisthokonts (which includes humans and the social amoeba Dictyostelium (Dd). Interestingly, Metazoa, unicellular Holozoa, and Fungi), Amoebozoa, and the evolutionarily distant MF myosins have similar roles in the exten- SAR (Stramenopiles, Alveolates, and Rhizaria) (Fig. 1 A and B). sion of actin-filled membrane protrusions such as filopodia and Over the course of hundreds of millions years of parallel evolution bind to microtubules (MT), suggesting that the core functions of the MF myosins have acquired or maintained roles in the formation these MF myosins have been highly conserved over evolution. -
Expression and Function of FERMT Genes in Colon Carcinoma Cells
ANTICANCER RESEARCH 33: 167-174 (2013) Expression and Function of FERMT Genes in Colon Carcinoma Cells KENJI KIRIYAMA1,2,3, YOSHIHIKO HIROHASHI1, TOSHIHIKO TORIGOE1, TERUFUMI KUBO1, YASUAKI TAMURA1, TAKAYUKI KANASEKI1, AKARI TAKAHASHI1, EMIRI NAKAZAWA1, ERI SAKA1, CHARLOTTE RAGNARSSON1, MUNEHIDE NAKATSUGAWA1, SATOKO INODA1,2, HIROKO ASANUMA4, HIDEO TAKASU5, TADASHI HASEGAWA4, TAKAHIRO YASOSHIMA3, KOICHI HIRATA2 and NORIYUKI SATO1 Department of 1Pathology, 2Surgery Ist and 4Surgical Pathology, Sapporo Medical University School of Medicine, Sapporo, Japan; 3Department of Surgery, Shinsapporo Keiaikai Hospital, Sapporo, Japan; 5Dainippon Sumitomo Pharma Co., Ltd., Osaka, Japan Abstract. Invasion into the matrix is one of hallmarks of Colon carcinoma is a major malignancy, with a high malignant diseases and is the first step for tumor metastasis. mortality rate. In the process of tumorigenesis, tumor cells Thus, analysis of the molecular mechanisms of invasion is undergo multiple steps of genetic events (1), and multiple essential to overcome tumor cell invasion. In the present study, steps are also required for the cells to obtain several different we screened for colon carcinoma-specific genes using a cDNA phenotypes. Tissue invasion and metastasis are hallmarks microarray database of colon carcinoma tissues and normal that distinguish malignant from benign diseases (2). Several colon tissues, and we found that fermitin family member-1 classes of proteins are involved in the process of tissue (FERMT1) is overexpressed in colon carcinoma cells. FRRMT1, invasion; however, the exact molecular mechanisms of FERMT2 and FERMT3 expression was investigated in colon invasion remain unclear. carcinoma cells. Reverse transcription polymerase chain Fermitin family member (FERMT) genes include FERMT1, reaction (RT-PCR) analysis revealed that only FERMT1 had FERMT2 and FERMT3, and these genes have been reported cancer cell-specific expression. -
Myth4 and FERM Have Overlapping and Distinct Roles in the Function of Myo1, a Class XIV Myosin in Tetrahymena Thermophila
City University of New York (CUNY) CUNY Academic Works All Dissertations, Theses, and Capstone Projects Dissertations, Theses, and Capstone Projects 2011 MyTH4 and FERM Have Overlapping and Distinct Roles in the Function of Myo1, a Class XIV Myosin in Tetrahymena thermophila Michael Gotesman Graduate Center, City University of New York How does access to this work benefit ou?y Let us know! More information about this work at: https://academicworks.cuny.edu/gc_etds/1643 Discover additional works at: https://academicworks.cuny.edu This work is made publicly available by the City University of New York (CUNY). Contact: [email protected] MyTH4 and FERM Have Overlapping and Distinct Roles in the Function of Myo1, a Class XIV Myosin in Tetrahymena thermophila By Michael Gotesman A dissertation submitted to the Graduate Faculty in Biology in partial fulfillment of the requirements for the degree of Doctor of Philosophy, The City University of New York 2011 This manuscript has been read and accepted for the Graduate Faculty in Biology in satisfaction of the dissertation requirements for the degree of Doctor of Philosophy. _____________ ________________________________________________ Date Chair of Examining Committee Dr. Ray H. Gavin, Brooklyn College _____________ ________________________________________________ Date Executive Officer Dr. Laurel A. Eckhardt ________________________________________________ Dr. Shaneen M. Singh, Brooklyn College ________________________________________________ Dr. Theodore R. Muth, Brooklyn College ________________________________________________ Dr. Chang-Hui Shen, College of Staten Island ________________________________________________ Dr. Selwyn A. Williams, New York City of Technology ________________________________________________ Dr. Christina King-Smith, Saint Joseph’s University Supervising Committee The City University of New York ii Abstract MyTH4 and FERM Have Overlapping and Distinct Roles in the Function of Myo1, a Class XIV Myosin in Tetrahymena thermophila By Michael Gotesman Adviser: Dr. -
Supplementary Materials
Supplementary materials Supplementary Table S1: MGNC compound library Ingredien Molecule Caco- Mol ID MW AlogP OB (%) BBB DL FASA- HL t Name Name 2 shengdi MOL012254 campesterol 400.8 7.63 37.58 1.34 0.98 0.7 0.21 20.2 shengdi MOL000519 coniferin 314.4 3.16 31.11 0.42 -0.2 0.3 0.27 74.6 beta- shengdi MOL000359 414.8 8.08 36.91 1.32 0.99 0.8 0.23 20.2 sitosterol pachymic shengdi MOL000289 528.9 6.54 33.63 0.1 -0.6 0.8 0 9.27 acid Poricoic acid shengdi MOL000291 484.7 5.64 30.52 -0.08 -0.9 0.8 0 8.67 B Chrysanthem shengdi MOL004492 585 8.24 38.72 0.51 -1 0.6 0.3 17.5 axanthin 20- shengdi MOL011455 Hexadecano 418.6 1.91 32.7 -0.24 -0.4 0.7 0.29 104 ylingenol huanglian MOL001454 berberine 336.4 3.45 36.86 1.24 0.57 0.8 0.19 6.57 huanglian MOL013352 Obacunone 454.6 2.68 43.29 0.01 -0.4 0.8 0.31 -13 huanglian MOL002894 berberrubine 322.4 3.2 35.74 1.07 0.17 0.7 0.24 6.46 huanglian MOL002897 epiberberine 336.4 3.45 43.09 1.17 0.4 0.8 0.19 6.1 huanglian MOL002903 (R)-Canadine 339.4 3.4 55.37 1.04 0.57 0.8 0.2 6.41 huanglian MOL002904 Berlambine 351.4 2.49 36.68 0.97 0.17 0.8 0.28 7.33 Corchorosid huanglian MOL002907 404.6 1.34 105 -0.91 -1.3 0.8 0.29 6.68 e A_qt Magnogrand huanglian MOL000622 266.4 1.18 63.71 0.02 -0.2 0.2 0.3 3.17 iolide huanglian MOL000762 Palmidin A 510.5 4.52 35.36 -0.38 -1.5 0.7 0.39 33.2 huanglian MOL000785 palmatine 352.4 3.65 64.6 1.33 0.37 0.7 0.13 2.25 huanglian MOL000098 quercetin 302.3 1.5 46.43 0.05 -0.8 0.3 0.38 14.4 huanglian MOL001458 coptisine 320.3 3.25 30.67 1.21 0.32 0.9 0.26 9.33 huanglian MOL002668 Worenine -
FRNK Regulatory Complex Formation with FAK Is Regulated by ERK Mediated Serine 217 Phosphorylation
Loyola University Chicago Loyola eCommons Dissertations Theses and Dissertations 2017 FRNK Regulatory Complex Formation with FAK Is Regulated by ERK Mediated Serine 217 Phosphorylation Taylor J. Zak Loyola University Chicago Follow this and additional works at: https://ecommons.luc.edu/luc_diss Part of the Biochemistry, Biophysics, and Structural Biology Commons Recommended Citation Zak, Taylor J., "FRNK Regulatory Complex Formation with FAK Is Regulated by ERK Mediated Serine 217 Phosphorylation" (2017). Dissertations. 2604. https://ecommons.luc.edu/luc_diss/2604 This Dissertation is brought to you for free and open access by the Theses and Dissertations at Loyola eCommons. It has been accepted for inclusion in Dissertations by an authorized administrator of Loyola eCommons. For more information, please contact [email protected]. This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License. Copyright © 2017 Taylor J. Zak LOYOLA UNIVERSITY CHICAGO FRNK REGULATORY COMPLEX FORMATION WITH FAK IS REGUALTED BY ERK MEDIATED SERINE 217 PHOSPHORYLATION A DISSERTATION SUBMITTED TO THE FACULTY OF THE GRADUATE SCHOOL IN CANDIDACY FOR THE DEGREE OF DOCTOR OF PHILOSOPHY PROGRAM IN CELL AND MOLECULAR PHYSIOLOGY BY TAYLOR J. ZAK CHICAGO, ILLINOIS MAY 2017 Copyright by Taylor J. Zak, 2017 All rights reserved. Dedicated to my wife Stacey ACKNOWLEDGEMENTS This dissertation would not be possible without the day to day guidance of doctors Seth Robia and Allen Samarel. Dr. Samarel’s guidance was missed during the final year of my dissertation as he transitioned to an emeritus professor and I am forever grateful to Dr. Robia for taking on some of Dr. Samarel’s role. -
ERM Protein Family
Cell Biology 2018; 6(2): 20-32 http://www.sciencepublishinggroup.com/j/cb doi: 10.11648/j.cb.20180602.11 ISSN: 2330-0175 (Print); ISSN: 2330-0183 (Online) Structure and Functions: ERM Protein Family Divine Mensah Sedzro 1, †, Sm Faysal Bellah 1, 2, †, *, Hameed Akbar 1, Sardar Mohammad Saker Billah 3 1Laboratory of Cellular Dynamics, School of Life Science, University of Science and Technology of China, Hefei, China 2Department of Pharmacy, Manarat International University, Dhaka, Bangladesh 3Department of Chemistry, Govt. M. M. University College, Jessore, Bangladesh Email address: *Corresponding author † These authors contributed equally to this work To cite this article: Divine Mensah Sedzro, Sm Faysal Bellah, Hameed Akbar, Sardar Mohammad Saker Billah. Structure and Functions: ERM Protein Family. Cell Biology . Vol. 6, No. 2, 2018, pp. 20-32. doi: 10.11648/j.cb.20180602.11 Received : September 15, 2018; Accepted : October 6, 2018; Published : October 29, 2018 Abstract: Preservation of the structural integrity of the cell depends on the plasma membrane in eukaryotic cells. Interaction between plasma membrane, cytoskeleton and proper anchorage influence regular cellular processes. The needed regulated connection between the membrane and the underlying actin cytoskeleton is therefore made available by the ERM (Ezrin, Radixin, and Moesin) family of proteins. ERM proteins also afford the required environment for the diffusion of signals in reactions to extracellular signals. Other studies have confirmed the importance of ERM proteins in different mode organisms and in cultured cells to emphasize the generation and maintenance of specific domains of the plasma membrane. An essential attribute of almost all cells are the specialized membrane domains. -
A Novel FERM Domain Including Guanine Nucleotide Exchange Factor Is Involved in Rac Signaling and Regulates Neurite Remodeling
The Journal of Neuroscience, October 1, 2002, 22(19):8504–8513 A Novel FERM Domain Including Guanine Nucleotide Exchange Factor Is Involved in Rac Signaling and Regulates Neurite Remodeling Tateki Kubo,1,2,3 Toshihide Yamashita,1,3 Atsushi Yamaguchi,1,3 Hideki Sumimoto,4 Ko Hosokawa,2 and Masaya Tohyama1,3 Departments of 1Anatomy and Neuroscience and 2Plastic Surgery, Osaka University Graduate School of Medicine, Suita, Osaka, 565-0871, Japan, 3Core Research for Evolutional Science and Technology of Japan Science and Technology Corporation, Kawaguchi, Saitama, 332-0012, Japan, and 4Medical Institute of Bioregulation, Kyushu University, Higashi-ku, Fukuoka 812-8582, Japan The Rho family of small GTPases, key regulators of the actin testis, as well as embryonic hippocampal and cortical neurons. cytoskeleton in eukaryotic cells from yeast to human, is impli- FIR was found to activate the biochemical pathway specific for cated in the control of neuronal morphology. Guanine nucleo- Rac1 but not for RhoA or Cdc42. Ectopic expression of FIR in tide exchange factors (GEFs) are upstream positive regulators the cortical neurons resulted in significantly shortened neurites of Rho GTPases and integrate extracellular signaling for appro- and excessive growth cones, presumably mediated by Rac1. priate activation of Rho GTPases at specific subcellular re- These results suggest that FIR may regulate neurite remodeling gions. Here we describe the identification of a novel Dbl family by mediating the signaling pathways from membrane proteins GEF for Rho GTPases in Homo sapiens and Mus musculus.It to Rac. contains a tandem Dbl homology–pleckstrin homology domain and FERM domain, characteristic of the plasma membrane Key words: Rac1; Rho guanine nucleotide exchange factor; proteins linker. -
FAK in Cancer: Mechanistic Findings and Clinical Applications
REVIEWS FAK in cancer: mechanistic findings and clinical applications Florian J. Sulzmaier, Christine Jean and David D. Schlaepfer Abstract | Focal adhesion kinase (FAK) is a cytoplasmic protein tyrosine kinase that is overexpressed and activated in several advanced-stage solid cancers. FAK promotes tumour progression and metastasis through effects on cancer cells, as well as stromal cells of the tumour microenvironment. The kinase-dependent and kinase-independent functions of FAK control cell movement, invasion, survival, gene expression and cancer stem cell self-renewal. Small molecule FAK inhibitors decrease tumour growth and metastasis in several preclinical models and have initial clinical activity in patients with limited adverse events. In this Review, we discuss FAK signalling effects on both tumour and stromal cell biology that provide rationale and support for future therapeutic opportunities. Focal Adhesion Kinase (FAK) is a multifunctional regu- models that have been used to elucidate new roles for lator of cell signalling within the tumour microenviron- FAK in endothelial cells (ECs) and discuss how stromal ment1–3. During development and in various tumours, FAK signalling contributes to tumour progression. FAK promotes cell motility, survival and proliferation Finally, we summarize new translational developments through kinase-dependent and kinase-independent using small molecule FAK inhibitors. mechanisms. In the past few years, Phase I and II clinical trials have been initiated with FAK inhibitors; however, FAK regulation some of the functions of FAK in tumorigenesis remain Control of FAK expression. Nuclear factor-κB (NF‑κB) under investigation. and p53 are well-characterized transcription factors that Chromosomal region 8q24.3, which encompasses activate and repress the PTK2 promoter, respectively10,11. -
Kindlin-3 Mutation in Mesenchymal Stem Cells Results in Enhanced Chondrogenesis
bioRxiv preprint doi: https://doi.org/10.1101/578690; this version posted March 15, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC 4.0 International license. Kindlin-3 Mutation in Mesenchymal Stem Cells Results in Enhanced Chondrogenesis Bethany A. Kerr1,2,3, Lihong Shi2, Alexander H. Jinnah3, Jeffrey S. Willey3,4, Donald P. Lennon5, Arnold I. Caplan5, Tatiana V. Byzova1 1 Department of Molecular Cardiology, Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Lerner Research Institute, Cleveland Clinic, Cleveland, Ohio, 44195 2 Department of Cancer Biology and Comprehensive Cancer Center, Wake Forest School of Medicine, Winston-Salem, NC 27157 3 Department of Orthopaedic Surgery, Wake Forest School of Medicine, Winston-Salem, NC 27157 4 Department of Radiation Biology, Wake Forest School of Medicine, Winston-Salem, NC 27157 5 Skeletal Research Center, Department of Biology, Case Western Reserve University, Cleveland, Ohio, 44106 Running Title: Kindlin-3 regulates chondrogenesis Address correspondence to: Bethany Kerr, Ph.D., Wake Forest School of Medicine, 1 Medical Center Blvd, Winston-Salem, NC, 27157. Telephone: 336-716-0320; Twitter: @BethanyKerrLab; e-mail: [email protected]; ORCID: 0000-0002-2995-7549 Number of Figures: 7 Number of Tables: 1 bioRxiv preprint doi: https://doi.org/10.1101/578690; this version posted March 15, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. -
Molecular Interactions of Talin and Actin: a Study on the Specific Domains of Talin Involved in the Interactions Ho-Sup Lee Iowa State University
Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 2002 Molecular interactions of talin and actin: a study on the specific domains of talin involved in the interactions Ho-Sup Lee Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Biochemistry Commons, Cell Biology Commons, and the Molecular Biology Commons Recommended Citation Lee, Ho-Sup, "Molecular interactions of talin and actin: a study on the specific domains of talin involved in the interactions " (2002). Retrospective Theses and Dissertations. 528. https://lib.dr.iastate.edu/rtd/528 This Dissertation is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Retrospective Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. INFORMATION TO USERS This manuscript has been reproduced from the microfilm master. UMI films the text directly from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter face, while others may be from any type of computer printer. The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleedthrough, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion. -
Human Caldag-GEFI Gene ( RASGRP2 ) Mutation Affects
Human CalDAG-GEFI gene ( RASGRP2 ) mutation affects platelet function and causes severe bleeding Matthias Canault, Dorsaf Ghalloussi, Charlotte Grosdidier, Marie Guinier, Claire Perret, Nadjim Chelghoum, Marine Germain, Hana Raslova, Franck Peiretti, Pierre E. Morange, et al. To cite this version: Matthias Canault, Dorsaf Ghalloussi, Charlotte Grosdidier, Marie Guinier, Claire Perret, et al.. Hu- man CalDAG-GEFI gene ( RASGRP2 ) mutation affects platelet function and causes severe bleed- ing. Journal of Experimental Medicine, Rockefeller University Press, 2014, 211 (7), pp.1349 - 1362. 10.1084/jem.20130477. hal-01478363 HAL Id: hal-01478363 https://hal.archives-ouvertes.fr/hal-01478363 Submitted on 27 May 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Distributed under a Creative Commons Attribution - NonCommercial - ShareAlike| 4.0 International License Published June 23, 2014 Article Human CalDAG-GEFI gene (RASGRP2) mutation affects platelet function and causes severe bleeding Matthias Canault,1,2,3 Dorsaf Ghalloussi,1,2,3 Charlotte Grosdidier,1,2,3 Marie Guinier,4 Claire Perret,5,6,7 Nadjim Chelghoum,4 Marine Germain,5,6,7 Hana Raslova,8 Franck Peiretti,1,2,3 Pierre E. Morange,1,2,3 Noemie Saut,1,2,3 Xavier Pillois,9,10 Alan T. -
FERM Domain Mediates Apical Targeting of PTP-BL 3301 and Incubating for 30 Minutes at Room Temperature
Journal of Cell Science 112, 3299-3308 (1999) 3299 Printed in Great Britain © The Company of Biologists Limited 1999 JCS0400 A FERM domain governs apical confinement of PTP-BL in epithelial cells Edwin Cuppen, Mietske Wijers, Jan Schepens, Jack Fransen, Bé Wieringa and Wiljan Hendriks* Department of Cell Biology, Institute of Cellular Signalling, University of Nijmegen, Adelbertusplein 1, 6525 EK Nijmegen, The Netherlands *Author for correspondence (e-mail: [email protected]) Accepted 2 July; published on WWW 22 September 1999 SUMMARY PTP-BL is a cytosolic multidomain protein tyrosine nor can we detect a direct interaction by phosphatase that shares homologies with several immunoprecipitation assays. Fluorescence recovery after submembranous and tumor suppressor proteins. Here we photobleaching (FRAP) experiments show that PTP-BL show, by transient expression of modular protein domains confinement is based on a dynamic steady state and that of PTP-BL in epithelial MDCK cells, that the presence of complete redistribution of the protein may occur within 20 a FERM domain in the protein is both necessary and minutes. Our observations suggest that relocation is sufficient for its targeting to the apical side of epithelial mediated via a cytosolic pool, rather than by lateral cells. Furthermore, immuno-electron microscopy on stable movement. Finally, we show that PTP-BL phosphatase expressing MDCK pools, that were obtained using an domains are involved in homotypic interactions, as EGFP-based cell sorting protocol, revealed that FERM demonstrated by yeast two-hybrid assays. Both the highly domain containing fusion proteins are enriched in restricted subcellular compartmentalization and its specific microvilli and have a typical submembranous location associative properties may provide the appropriate at about 10-15 nm from the plasma membrane.