phosphorylation of E-cadherin molecules

Patrick F.H. Lai pfhlai at LOOKSMART.COM
Sun Jul 12 09:02:39 EST 1998


---- Begin Original Message from THX ----
I'm looking some informations about the regulation of E-cadherin expres=
sion
by phosphorylation. When E-cadherin is phosphoryled, is-it functionnal?=

is-it the contrary? Please help me...

---- End Original Message ----

Dear THX,

Based on the following abstract, the phorsphorylation state of 
E-cadherin appeared to be very important to its function.

=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=
=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D
A short core region of E-cadherin is essential for catenin binding
 and is highly phosphorylated.
by Stappert J & Kemler R
Max-Planck-Institut f=FCr Immunbiologie, Freiburg.
Cell Adhes Commun 1994 Aug 2:4 319-27

Abstract
Classical cadherins associate with three cytoplasmic proteins, termed
 alpha, -beta- and gamma-catenin. This association
mediates the attachment of cadherins to the microfilament network, 
which is believed to be of major importance for cadherin
function. Deletion of the carboxyterminal 72-amino acid residues of
 E-cadherin had been previously shown to prevent catenin
binding. Here we have analyzed additional mutants of E-cadherin with de=
letions within this region and identified a core region of
30 amino acids (E-cadherin pos. 832-862) essential for the 
interaction with catenins. Phosphorylation analysis of wild-type and
mutant E-cadherin indicates that the catenin-binding domain is highly
 phosphorylated. In particular, the 30 amino acid region
contains 8 serine residues which are well conserved among cadherins.
 To elucidate whether phosphorylation might be important
for cadherin-catenin complex formation, site-directed mutagenesis
 experiments were performed. Partial substitutions of up to 5
of the 8 serine residues in the cluster had no influence on
 E-cadherin-catenin complex formation and E-cadherin mediated cell
adhesion, although phosphorylation of E-cadherin was reduced. In
 contrast, substitution of the whole serine cluster completely
abolished phosphorylation and affected complex formation with
 catenins. These results suggest that E-cadherin-catenin
interaction may be regulated by phosphorylation of the catenin-
binding domain, which might represent one molecular
mechanism to regulate cadherin mediated cell adhesion.

=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=
=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=


Try Medine with 'E-cadherin' AND 'phorsphorylation'.
You'll get tonnes of relevant stuffs.
Good luck.





Hope this is useful info.   :-)


Patrick F.H. Lai  
Graduate Student, University of Toronto 
< PFHLai at looksmart.com >




     
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