Villin-type headpiece domains show a wide range of F-actin-binding affinities.
Cell Motil Cytoskeleton
; 52(1): 9-21, 2002 May.
Article
in En
| MEDLINE
| ID: mdl-11977079
ABSTRACT
The villin-type "headpiece" domain is a modular motif found at the extreme C-terminus of larger "core" domains in over 25 cytoskeletal proteins in plants and animals. Although headpiece is classified as an F-actin-binding domain, it has been suggested that some expressed fusion-proteins containing headpiece may lack F-actin-binding in vivo. To determine the intrinsic F-actin affinity of headpiece domains, we quantified the F-actin affinity of seven headpiece domains and three N-terminal truncations, under identical in vitro conditions. The constructs are folded and adopt the native headpiece structure. However, they show a wide range of affinities that can be grouped into high, low, and nonspecific-binding categories. Computer models of the structure and charged surface potential of these headpiece domains suggest features important for high F-actin affinity. We conclude that not all headpiece domains are intrinsically F-actin-binding motifs, and suggest that the surface charge distribution may be an important element for F-actin recognition.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Carrier Proteins
/
Actins
/
Microfilament Proteins
Limits:
Animals
Language:
En
Journal:
Cell Motil Cytoskeleton
Year:
2002
Document type:
Article
Affiliation country:
United States