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Sökning: onr:"swepub:oai:DiVA.org:kth-271764" > Cells Control BIN1-...
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03480naa a2200373 4500 | |
| 001 | oai:DiVA.org:kth-271764 | |
| 003 | SwePub | |
| 008 | 200407s2020 | |||||||||||000 ||eng| | |
| 009 | oai:prod.swepub.kib.ki.se:143207365 | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-2717642 URI |
| 024 | 7 | a https://doi.org/10.1016/j.jmb.2019.12.0012 DOI |
| 024 | 7 | a http://kipublications.ki.se/Default.aspx?queryparsed=id:1432073652 URI |
| 040 | a (SwePub)kthd (SwePub)ki | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Gowrisankaran, Sindhujau European Neurosci Inst, Synapt Vesicle Dynam Grp, Gottingen, Germany.4 aut |
| 245 | 1 0 | a Cells Control BIN1-Mediated Membrane Tubulation by Altering the Membrane Charge |
| 264 | 1 | b ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD,c 2020 |
| 338 | a print2 rdacarrier | |
| 500 | a QC 20200407 | |
| 520 | a The Bridging integrator 1 (BIN1)/Amphiphysin/Rvs (BAR) protein family is an essential part of the cell's machinery to bend membranes. BIN1 is a muscle-enriched BAR protein with an established role in muscle development and skeletal myopathies. Here, we demonstrate that BIN1, on its own, is able to form complex interconnected tubular systems in vitro, reminiscent of t-tubule system in muscle cells. We further describe how BIN1's electrostatic interactions regulate membrane bending: the ratio of negatively charged lipids in the bilayer altered membrane bending and binding properties of BIN1 and so did the manipulation of BIN1's surface charge. We show that the electrostatically mediated BIN1 membrane binding depended on the membrane curvature-it was less affected in liposomes with high curvature. Curiously, BIN1 membrane binding and bending was diminished in cells where the membrane's charge was experimentally reduced. Membrane bending was also reduced in BIN1 mutants where negative or positive charges in the BAR domain have been eliminated. This phenotype, characteristic of BIN1 mutants linked to myopathies, was rescued when the membrane charge was made more negative. The latter findings also show that cells can control tubulation at their membranes by simply altering the membrane charge and through it, the recruitment of BAR proteins and their interaction partners (e.g. dynamin). | |
| 650 | 7 | a MEDICIN OCH HÄLSOVETENSKAPx Medicinsk bioteknologi0 (SwePub)3042 hsv//swe |
| 650 | 7 | a MEDICAL AND HEALTH SCIENCESx Medical Biotechnology0 (SwePub)3042 hsv//eng |
| 700 | 1 | a Wang, Zuonengu KTH,Strukturell bioteknik,Karolinska Inst, Dept Nutr & Biosci, Huddinge, Sweden.4 aut0 (Swepub:kth)u1jskro6 |
| 700 | 1 | a Morgan, David G.u Indiana Univ, Electron Microscopy Ctr, Bloomington, IN USA.4 aut |
| 700 | 1 | a Milosevic, Irau European Neurosci Inst, Synapt Vesicle Dynam Grp, Gottingen, Germany.4 aut |
| 700 | 1 | a Mim, Carstenu KTH,Strukturell bioteknik,Karolinska Inst, Dept Nutr & Biosci, Huddinge, Sweden.4 aut0 (Swepub:kth)u1ce0qjf |
| 710 | 2 | a European Neurosci Inst, Synapt Vesicle Dynam Grp, Gottingen, Germany.b Strukturell bioteknik4 org |
| 773 | 0 | t Journal of Molecular Biologyd : ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTDg 432:4, s. 1235-1250q 432:4<1235-1250x 0022-2836x 1089-8638 |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-271764 |
| 856 | 4 8 | u https://doi.org/10.1016/j.jmb.2019.12.001 |
| 856 | 4 8 | u http://kipublications.ki.se/Default.aspx?queryparsed=id:143207365 |
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