Imaging protein-protein interactions in cell motility using fluorescence resonance energy transfer (FRET)

M Parsons; B Vojnovic; S Ameer-Beg

Imaging protein-protein interactions in cell motility using fluorescence resonance energy transfer (FRET)

M Parsons^*, B Vojnovic, S Ameer-Beg

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

52 Citations (Scopus)

Abstract

Protein-protein interactions and signal transduction pathways have traditionally been analysed using biochemical techniques or standard microscopy. Although invaluable in the delineation of protein hierarchy, these methods do not provide information on the true spatial and temporal nature of complex formation within the intact cell. Recent advances in microscopy have allowed the development of new methods to analyse protein-protein interactions at very high resolution in both fixed and live cells. The present paper provides a brief overview of using fluorescence resonance energy transfer to analyse directly molecular interactions and conformational changes in various proteins involved in the regulation of cell adhesion and motility.

Original language	English
Article number	N/A
Pages (from-to)	431-433
Number of pages	3
Journal	Biochemical Society Transactions
Volume	32
Issue number	3
Publication status	Published - Jun 2004
Event	Meeting on the Molecular Environment of Integrins - Manchester, ENGLAND Duration: 1 Jan 2004 → …

Keywords

actin cytoskelelon
cell migration
fluorescence lifetime imaging microscopy (FLIM)
fluorescence resonance energy transfer (FRET)
signalling
KINASE-C-ALPHA
MICROSCOPY

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title = "Imaging protein-protein interactions in cell motility using fluorescence resonance energy transfer (FRET)",

abstract = "Protein-protein interactions and signal transduction pathways have traditionally been analysed using biochemical techniques or standard microscopy. Although invaluable in the delineation of protein hierarchy, these methods do not provide information on the true spatial and temporal nature of complex formation within the intact cell. Recent advances in microscopy have allowed the development of new methods to analyse protein-protein interactions at very high resolution in both fixed and live cells. The present paper provides a brief overview of using fluorescence resonance energy transfer to analyse directly molecular interactions and conformational changes in various proteins involved in the regulation of cell adhesion and motility.",

keywords = "actin cytoskelelon, cell migration, fluorescence lifetime imaging microscopy (FLIM), fluorescence resonance energy transfer (FRET), signalling, KINASE-C-ALPHA, MICROSCOPY",

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year = "2004",

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language = "English",

volume = "32",

pages = "431--433",

journal = "Biochemical Society Transactions",

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T1 - Imaging protein-protein interactions in cell motility using fluorescence resonance energy transfer (FRET)

AU - Parsons, M

AU - Vojnovic, B

AU - Ameer-Beg, S

PY - 2004/6

Y1 - 2004/6

N2 - Protein-protein interactions and signal transduction pathways have traditionally been analysed using biochemical techniques or standard microscopy. Although invaluable in the delineation of protein hierarchy, these methods do not provide information on the true spatial and temporal nature of complex formation within the intact cell. Recent advances in microscopy have allowed the development of new methods to analyse protein-protein interactions at very high resolution in both fixed and live cells. The present paper provides a brief overview of using fluorescence resonance energy transfer to analyse directly molecular interactions and conformational changes in various proteins involved in the regulation of cell adhesion and motility.

AB - Protein-protein interactions and signal transduction pathways have traditionally been analysed using biochemical techniques or standard microscopy. Although invaluable in the delineation of protein hierarchy, these methods do not provide information on the true spatial and temporal nature of complex formation within the intact cell. Recent advances in microscopy have allowed the development of new methods to analyse protein-protein interactions at very high resolution in both fixed and live cells. The present paper provides a brief overview of using fluorescence resonance energy transfer to analyse directly molecular interactions and conformational changes in various proteins involved in the regulation of cell adhesion and motility.

KW - actin cytoskelelon

KW - cell migration

KW - fluorescence lifetime imaging microscopy (FLIM)

KW - fluorescence resonance energy transfer (FRET)

KW - signalling

KW - KINASE-C-ALPHA

KW - MICROSCOPY

UR - http://www.scopus.com/inward/record.url?scp=3042660199&partnerID=8YFLogxK

M3 - Article

SN - 1470-8752

VL - 32

SP - 431

EP - 433

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

IS - 3

M1 - N/A

T2 - Meeting on the Molecular Environment of Integrins

Y2 - 1 January 2004

ER -

Imaging protein-protein interactions in cell motility using fluorescence resonance energy transfer (FRET)

Abstract

Keywords

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