Johanna Ivaska

ORCID: 0000-0002-6295-6556
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About
Contact & Profiles
Research Areas
  • Cell Adhesion Molecules Research
  • Cellular Mechanics and Interactions
  • Cellular transport and secretion
  • Cancer Cells and Metastasis
  • 3D Printing in Biomedical Research
  • Hippo pathway signaling and YAP/TAZ
  • Protease and Inhibitor Mechanisms
  • Ubiquitin and proteasome pathways
  • Caveolin-1 and cellular processes
  • Microtubule and mitosis dynamics
  • HER2/EGFR in Cancer Research
  • Phagocytosis and Immune Regulation
  • Angiogenesis and VEGF in Cancer
  • Protein Kinase Regulation and GTPase Signaling
  • Monoclonal and Polyclonal Antibodies Research
  • Signaling Pathways in Disease
  • Protein Tyrosine Phosphatases
  • Skin and Cellular Biology Research
  • Cancer, Hypoxia, and Metabolism
  • Melanoma and MAPK Pathways
  • Cancer-related Molecular Pathways
  • Wnt/β-catenin signaling in development and cancer
  • Peptidase Inhibition and Analysis
  • Cancer Research and Treatments
  • Glycosylation and Glycoproteins Research

University of Turku
2016-2025

Åbo Akademi University
2016-2025

Turku Centre for Computer Science
2019-2025

Cancer Society of Finland
2022-2025

Turku University Hospital
2023-2024

VTT Technical Research Centre of Finland
2007-2023

Cancer Institute (WIA)
2022-2023

Turku Centre for Biotechnology
2013-2022

History of Science Society
2022

Inserm
2019

Significance The central concept in this study is that a major cytoskeletal component, vimentin, acts as signal integrator during wound healing, operating both signal-triggering and signal-receiving cells. This previously unreported for intermediate filaments, with an evolving paradigm according to which filaments emerge integrators of regeneration specific functions the particular tissues individual are characteristic. Our reveals underlying molecular cellular control vimentin...

10.1073/pnas.1519197113 article EN cc-by Proceedings of the National Academy of Sciences 2016-07-08

In the integrin family, collagen receptors form a structurally and functionally distinct subgroup. Two members of this subgroup, α1β1 α2β1 integrins, are known to bind monomeric type I collagen. However, in tissues monomers organized into large fibrils immediately after they released from cells. Here, we studied fibril recognition by integrins. By an immunoelectron microscopy method showed that α2I domain is able classical D-banded fibrils. according solid phase binding assay, formation...

10.1074/jbc.m401409200 article EN cc-by Journal of Biological Chemistry 2004-07-01

Dynamic turnover of integrin cell adhesion molecules to and from the surface is central migration. We report for first time an association between integrins Rab proteins, which are small GTPases involved in traffic endocytotic vesicles. Rab21 (and Rab5) associate with cytoplasmic domains α-integrin chains, their expression influences endo/exocytic integrins. This function dependent on its GTP/GDP cycle proper membrane targeting. Knock down impairs integrin-mediated motility, whereas...

10.1083/jcb.200509019 article EN The Journal of Cell Biology 2006-06-05

Angiopoietins regulate vascular homeostasis via the endothelial Tie receptor tyrosine kinases. Angiopoietin-1 (Ang1) supports stabilization Tie2 activation. Angiopoietin-2 (Ang2) functions as a context-dependent agonist/antagonist promoting pathological angiogenesis, permeability and inflammation. Elucidating Ang2-dependent mechanisms of destablization is critical for rational design angiopoietin antagonists that have demonstrated therapeutic efficacy in cancer trials. Here, we report Ang2,...

10.1038/ncomms6962 article EN cc-by Nature Communications 2015-01-30

Integrin trafficking plays an important role in cellular motility and cytokinesis. Integrins undergo constant endo/exocytic shuttling to facilitate the dynamic regulation of cell adhesion. activity toward components extracellular matrix is regulated by ability these receptors switch between active inactive conformations. Several signalling pathways have been described integrin traffic under different conditions. However, interrelationship conformations their endocytic fate remained...

10.1111/j.1600-0854.2012.01327.x article EN Traffic 2012-01-06

Abstract Purpose: To investigate the clinical relevance of recently characterized human oncoprotein cancerous inhibitor protein phosphatase 2A (CIP2A) in breast cancer. Experimental Design: CIP2A expression (mRNA and protein) was measured three different sets mammary tumors compared with clinicopathologic variables. The functional role cancer cells evaluated by small interfering RNA–mediated depletion followed an analysis cell proliferation, migration, anchorage-independent growth, xenograft...

10.1158/1078-0432.ccr-08-3283 article EN Clinical Cancer Research 2009-08-12

ABSTRACT Echovirus 1 (EV1) is a human pathogen which belongs to the Picornaviridae family of RNA viruses. We have analyzed early events infection after EV1 binding its receptor α2β1 integrin and elucidated route by gains access host cell. onto cell surface subsequent entry resulted in conformational changes viral capsid as demonstrated sucrose gradient sedimentation analysis. After 15 min 2 h postinfection (p.i.) proteins were seen vesicular structures that negative for markers...

10.1128/jvi.76.4.1856-1865.2002 article EN Journal of Virology 2002-02-15

Two collagen receptors, integrins α1β1 and α2β1, can regulate distinct functions in cells. Ligation of α1β1, unlike has been shown to result recruitment Shc activation the Ras/ERK pathway. To identify downstream signaling molecules activated by α2β1 integrin, we have overexpressed wild-type α2, or chimeric α2 subunit with α1 integrin cytoplasmic domain human osteosarcoma cells (Saos-2) lacking endogenous α2β1. The α2/α1 chain formed a functional heterodimer β1. In contrast chimera, forced...

10.1083/jcb.147.2.401 article EN The Journal of Cell Biology 1999-10-18
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