English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  LOVTRAP: an optogenetic system for photoinduced protein dissociation

Wang, H., Vilela, M., Winkler, A., Tarnawski, M., Schlichting, I., Yumerefendi, H., et al. (2016). LOVTRAP: an optogenetic system for photoinduced protein dissociation. Nature methods, 13(9), 755-758. doi:10.1038/nmeth.3926.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-1FDA-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-9CC7-9
Genre: Journal Article

Files

show Files
hide Files
:
NatMeth_epup_2016_926.pdf (Any fulltext), 2MB
 
File Permalink:
-
Name:
NatMeth_epup_2016_926.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
NatMeth_epup_2016_926_Suppl.pdf (Supplementary material), 3MB
 
File Permalink:
-
Name:
NatMeth_epup_2016_926_Suppl.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
Locator:
https://dx.doi.org/10.1038/nmeth.3926 (Any fulltext)
Description:
-
Description:
-
Description:
-

Creators

show
hide
 Creators:
Wang, Hui, Author
Vilela, Marco, Author
Winkler, Andreas1, Author              
Tarnawski, Miroslaw1, Author              
Schlichting, Ilme1, Author              
Yumerefendi, Hayretin, Author
Kuhlman, Brian, Author
Liu, Rihe, Author
Danuser, Gaudenz, Author
Hahn, Klaus M, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Content

show
hide
Free keywords: Cell migration; Cell signalling; Optogenetics
 Abstract: LOVTRAP is an optogenetic approach for reversible light-induced protein dissociation using protein A fragments that bind to the LOV domain only in the dark, with tunable kinetics and a >150-fold change in the dissociation constant (Kd). By reversibly sequestering proteins at mitochondria, we precisely modulated the proteins' access to the cell edge, demonstrating a naturally occurring 3-mHz cell-edge oscillation driven by interactions of Vav2, Rac1, and PI3K proteins.

Details

show
hide
Language(s): eng - English
 Dates: 2016-06-162015-11-212016-07-182016-09-01
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature methods
  Other : Nature methods
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: New York, NY : Nature Pub. Group
Pages: - Volume / Issue: 13 (9) Sequence Number: - Start / End Page: 755 - 758 Identifier: ISSN: 1548-7091
CoNE: https://pure.mpg.de/cone/journals/resource/111088195279556