Search results for "integriini"
showing 10 items of 22 documents
Phosphorylated immunoreceptor tyrosine-based activation motifs and integrin cytoplasmic domains activate spleen tyrosine kinase via distinct mechanis…
2018
Spleen tyrosine kinase (Syk) is involved in cellular adhesion and also in the activation and development of hematopoietic cells. Syk activation induced by genomic rearrangement has been linked to certain T-cell lymphomas, and Syk inhibitors have been shown to prolong survival of patients with B-cell lineage malignancies. Syk is activated either by its interaction with a double-phosphorylated immunoreceptor tyrosine-based activation motif (pITAM), which induces rearrangements in the Syk structure, or by the phosphorylation of specific tyrosine residues. In addition to its immunoreceptor function, Syk is activated downstream of integrin pathways, and integrins bind to the same region in Syk a…
Binding properties and stability of the Ras-association domain of Rap1-GTP interacting adapter molecule (RIAM).
2012
The Rap1-GTP interacting adapter protein (RIAM) is an important protein in Rap1-mediated integrin activation. By binding to both Rap1 GTPase and talin, RIAM recruits talin to the cell membrane, thus facilitating talin-dependent integrin activation. In this article, we studied the role of the RIAM Ras-association (RA) and pleckstrin-homology (PH) domains in the interaction with Rap1. We found that the RA domain was sufficient for GTP-dependent interaction with Rap1B, and the addition of the PH domain did not change the binding affinity. We also detected GTP-independent interaction of Rap1B with the N-terminus of RIAM. In addition, we found that the PH domain stabilized the RA domain both in …
Structures, interactions and packing of filamin domains
2011
Echovirus 1 infektion vaikutus epidermaalisen kasvutekijäreseptorin endosytoosiin ja signalointiin
2013
Epidermaalinen kasvutekijäreseptori (EGFR) on yhdessä kollageeni- ja lamiinireseptori α2β1-integriinin kanssa tärkeä tekijä solun selviytymisen, kiinnittymisen ja jakautumisen säätelemisessä sekä syöpäsoluissa. Kasvutekijän sitoutumisen jälkeen EGFR:t dimerisoituvat, endosytoituvat klatriinivälitteisen endosytoosin kautta ja kulkeutuvat solun sisällä kolmen eri reitin mukaisesti: 1) EGFR-ligandi-kompleksi voi ubikitinaation seurauksena päätyä lysosomaaliseen pH:sta riippuvaan hajoitukseen, EGFR kierrättyy takaisin solukalvolle 2) ligandin irtoamisen tai 3) UBPY de-ubikitinaatioenstyymin toimesta. α2β1-integriinireseptori klusteroituu solukalvolle kiinnityttyään kollageeniin, lamiiniin, Echo…
Endosomin sisäisen ioniympäristön vaikutukset echovirus 1 -infektioon
2009
Cholesterol Dependence of Collagen and Echovirus 1 Trafficking along the Novel alpha2beta1 Integrin Internalization Pathway
2013
We have previously shown that soluble collagen and a human pathogen, echovirus 1 (EV1) cluster α2β1 integrin on the plasma membrane and cause their internalization into cytoplasmic endosomes. Here we show that cholesterol plays a major role not only in the uptake of α2β1 integrin and its ligands but also in the formation of α2 integrin-specific multivesicular bodies (α2-MVBs) and virus infection. EV1 infection and α2β1 integrin internalization were totally halted by low amounts of the cholesterol-aggregating drugs filipin or nystatin. Inhibition of cholesterol synthesis and accumulation of lanosterol after ketoconazole treatment inhibited uptake of collagen, virus and clustered integrin, an…
Integrin-mediated entry of echovirus 1
2008
Paula Upla selvitti väitöskirjassaan echovirus 1:n solunsisäistä reittiä ja tunnisti solurakenteita ja säätelijöitä, jotka ovat tärkeitä infektiossa. Echovirus 1 (EV1) kuuluu pikornavirusperheeseen, jonka muita tunnettuja edustajia ovat poliovirus sekä karjan suu- ja sorkkatautivirus. EV1 on pieni (25-30 nm), vaipaton RNA-virus. EV1 aiheuttaa useimmiten oireettomia tai vähäoireisia suolisto- ja hengitystieinfektioita, mutta myös vakavampia tiloja, kuten aivokalvontulehdusta.Upla seurasi viruksen tunkeutumista soluun käyttäen elektronimikroskopiaa sekä tehokasta kolmi- ja neliulotteista konfokaalimikroskopiaa. Näin hän pystyi havainnoimaan yhtä aikaa usean eri molekyylin vuorovaikutusta niih…
Binding Properties and Stability of the Ras-Association Domain of Rap1-GTP Interacting Adapter Molecule (RIAM)
2012
The Rap1-GTP interacting adapter protein (RIAM) is an important protein in Rap1-mediated integrin activation. By binding to both Rap1 GTPase and talin, RIAM recruits talin to the cell membrane, thus facilitating talin-dependent integrin activation. In this article, we studied the role of the RIAM Ras-association (RA) and pleckstrin-homology (PH) domains in the interaction with Rap1. We found that the RA domain was sufficient for GTP-dependent interaction with Rap1B, and the addition of the PH domain did not change the binding affinity. We also detected GTP-independent interaction of Rap1B with the N-terminus of RIAM. In addition, we found that the PH domain stabilized the RA domain both in …