FRET and FRAP imaging: Approaches to characterise tau and stathmin interactions with microtubules in cells. (15th February 2013)
- Record Type:
- Journal Article
- Title:
- FRET and FRAP imaging: Approaches to characterise tau and stathmin interactions with microtubules in cells. (15th February 2013)
- Main Title:
- FRET and FRAP imaging: Approaches to characterise tau and stathmin interactions with microtubules in cells
- Authors:
- Nouar, Roqiya
Devred, François
Breuzard, Gilles
Peyrot, Vincent - Abstract:
- Abstract: Microtubules (MTs) are involved in many crucial processes such as cell morphogenesis, mitosis and motility. These dynamic structures resulting from the complex assembly of tubulin are tightly regulated by stabilising MT‐associated proteins (MAPs) such as tau and destabilising proteins, notably stathmin. Because of their key role, these MAPs and their interactions have been extensively studied using biochemical and biophysical approaches, particularly in vitro . Nevertheless, numerous questions remain unanswered and the mechanisms of interaction between MT and these proteins are still unclear in cells. Techniques coupling cell imaging and fluorescence methods, such as Förster resonance energy transfer and fluorescence recovery after photobleaching, are excellent tools to study these interactions in situ . After describing these methods, we will present emblematic data from the literature and unpublished experimental results from our laboratory concerning the interactions between MTs, tau and stathmin in cells. Abstract : The dynamic behaviour of microtubules (MTs) is finely regulated by interactions with MT‐associated proteins. These interactions have been extensively studied in vitro by biochemical and structural approaches, but remain difficult to investigate in a cellular context mainly due to poorly adapted methods. Advanced fluorescence techniques such as Förster resonance energy transfer and fluorescence recovery after photobleaching are appropriatedAbstract: Microtubules (MTs) are involved in many crucial processes such as cell morphogenesis, mitosis and motility. These dynamic structures resulting from the complex assembly of tubulin are tightly regulated by stabilising MT‐associated proteins (MAPs) such as tau and destabilising proteins, notably stathmin. Because of their key role, these MAPs and their interactions have been extensively studied using biochemical and biophysical approaches, particularly in vitro . Nevertheless, numerous questions remain unanswered and the mechanisms of interaction between MT and these proteins are still unclear in cells. Techniques coupling cell imaging and fluorescence methods, such as Förster resonance energy transfer and fluorescence recovery after photobleaching, are excellent tools to study these interactions in situ . After describing these methods, we will present emblematic data from the literature and unpublished experimental results from our laboratory concerning the interactions between MTs, tau and stathmin in cells. Abstract : The dynamic behaviour of microtubules (MTs) is finely regulated by interactions with MT‐associated proteins. These interactions have been extensively studied in vitro by biochemical and structural approaches, but remain difficult to investigate in a cellular context mainly due to poorly adapted methods. Advanced fluorescence techniques such as Förster resonance energy transfer and fluorescence recovery after photobleaching are appropriated techniques to characterise the interactions between MTs and their associated proteins such as tau or stathmin directly in cells. … (more)
- Is Part Of:
- Biology of the cell. Volume 105:Number 4(2013:Apr.)
- Journal:
- Biology of the cell
- Issue:
- Volume 105:Number 4(2013:Apr.)
- Issue Display:
- Volume 105, Issue 4 (2013)
- Year:
- 2013
- Volume:
- 105
- Issue:
- 4
- Issue Sort Value:
- 2013-0105-0004-0000
- Page Start:
- 149
- Page End:
- 161
- Publication Date:
- 2013-02-15
- Subjects:
- FRAP -- FRET -- Microtubules -- Stathmin -- Tau
Cytology -- Periodicals
Electron microscopy -- Periodicals
571.6 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1111/boc.201200060 ↗
- Languages:
- English
- ISSNs:
- 0248-4900
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 2087.045000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 1287.xml