TABLE 21-6
Ac tin—
Cross- Linking Proteins
* *
Protein*
MW
Domain Organization
G
roup
1
30 Kd
33,000
EF-la
50,(KX)
Fuse
in
55.000
Scruin
102.000
G
roup
II
Villin
92.(XX)
Dcmatin
48.000
G
roup
III
Fimbrin
68.000
0
=
0
»
CD
C D
ot-Actinin
102.000
Spectrin
a: 280.000
|3: 246,000—
275.000
Dystrophin
427.(K)0
ABP120
92.000
Filamin
280.(KK)
Location
Filopodia. lamellipodia. stress tibers
Pseudopodia
Filopodia. lamellipodia. stress tibers.
microvilli, acrosomal process
Acrosomal process
Intestinal and kidney brush border
microvilli
Erythr<KVte cortical network
Microvilli, stereocilia, adhesion
plaques, yeast actin cables
Filopodia. lamellipodia. stress libers,
adhesion plaques
Cortical networks
Muscle cortical networks
Pseudopodia
Filopodia. pseudopodia, stress libers
“Cross-linking proteins are placed into three groups. Group I proteins have unique actin-binding domains: Group II have a 7.000-MW aetin-binding
domain: and Group III have pairs of a 26.tX)0-MW aetin-binding domain.
Calmodulin-like calcium-binding domains (light blue!, actin-binding domains (dark blue).
Actin-Capping and Actin-Severing Proteins
* *
Protein
MW
Domain Organization*
Activity
gCAP39
40.000
c c o
Capping
Severin (fragmin)’
40.000
CCD
Capping, severing
Gelsolin
87.000
Capping, severing
Villin
92.(XK)
Capping, severing, cross-linking
*Aetin monomer binding domains are white; F-actin binding domains are shaded.
i'Sevcrin and fragmin are synonyms for the same protein.
Reproduced with permission from: It Lodish <7
nl. M olecu lar C ell Hiolotty,
5rd edition. W. H. Freeman and Co.
. New York 1995 Page 997 and
page I1HI9.
