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VERSION:2.0
CALSCALE:GREGORIAN
METHOD:PUBLISH
BEGIN:VEVENT
DTSTAMP:20141124T093939Z
DTSTART:20141125T130000Z
DTEND:20141125T140000Z
SUMMARY:Regulation of actin assembly and mechanotransduction in cell-matr
 ix adhesion complexes: a biochemical study of the talin-vinculin complex
 
UID:{http://www.columbasystems.com/customers/uom/gpp/eventid/}g63-i0pcgax
 1-ciaocv
DESCRIPTION:This seminar is part of the Tissue Systems seminar series.   
                                                                         
                                                                         
                                          Cell migration is involved in m
 any physiological and pathological processes. Cells use the force produc
 ed by actin polymerization and actomyosin contraction for movement. To p
 roduce force\, the actin cytoskeleton is mechanically coupled to the ext
 racellular matrix (ECM). Actin binding proteins (ABPs)\, frequently clus
 tered in adhesion complexes\, play a critical role in ECM-actin coupling
 . Among the few ABPs that have been characterised in adhesion complexes\
 , some proteins regulate actin nucleation\, association and elongation. 
 Others proteins modulate actin binding and dynamics in a mechanosensitiv
 e manner. Our goal is to determine the molecular mechanisms by which the
 se ABPs cooperate to control actin anchoring in adhesion complexes\, and
  consequently migration speed. \nTo study these ABPs\, our laboratory co
 mbines the measurement of actin polymerisation kinetics in fluorescence 
 spectroscopy\, single actin filament observations in TIRF microscopy and
  the reconstitution of actin-based mechanosensitive processes on micropa
 tterned surfaces. \nOur results showed that vinculin controls actin fila
 ment elongation. More recent results revealed that talin also regulates 
 actin polymerisation. In addition\, we have developed a microscopy assay
  with pure proteins in which the self-assembly of actomyosin cables cont
 rols the association of vinculin to a talin-micropatterned surface in a 
 reversible manner. This in vitro reconstitution revealed the mechanism b
 y which a key molecular switch senses and controls the connection betwee
 n adhesion complexes and the actomyosin cytoskeleton.\n
STATUS:TENTATIVE
TRANSP:TRANSPARENT
CLASS:PUBLIC
LOCATION:Lecture Theatre\, Michael Smith Building\, Manchester
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