Abstract
The function of the NF2 tumor suppressor merlin has remained elusive despite increasing evidence for its role in actin cytoskeleton reorganization. The closely related ERM proteins (ezrin, radixin, and moesin) act as linkers between the cell membrane and cytoskeleton, and have also been implicated as active actin reorganizers. We report here that merlin and the ERMs can interact with and regulate N-WASP, a critical regulator of actin dynamics. Merlin and moesin were found to inhibit N-WASP-mediated actin assembly in vitro, a function that appears independent of their ability to bind actin. Furthermore, exogenous expression of a constitutively active ERM inhibits N-WASP-dependent Shigella tail formation, suggesting that the ERMs may function as inhibitors of N-WASP function in vivo. This novel function of merlin and the ERMs illustrates a mechanism by which these proteins directly exert their effects on actin reorganization and also provides new insight into N-WASP regulation.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 12517-12522 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 280 |
| Issue number | 13 |
| DOIs | |
| State | Published - Apr 1 2005 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
The NF2 tumor suppressor merlin and the ERM proteins interact with N-WASP and regulate its actin polymerization function. / Manchanda, Nitasha; Lyubimova, Anna; Ho, Hsin-Yi Henry; James, Marianne F.; Gusella, James F.; Ramesh, Narayanaswamy; Snapper, Scott B.; Ramesh, Vijaya.
In: Journal of Biological Chemistry, Vol. 280, No. 13, 01.04.2005, p. 12517-12522.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The NF2 tumor suppressor merlin and the ERM proteins interact with N-WASP and regulate its actin polymerization function
AU - Manchanda, Nitasha
AU - Lyubimova, Anna
AU - Ho, Hsin-Yi Henry
AU - James, Marianne F.
AU - Gusella, James F.
AU - Ramesh, Narayanaswamy
AU - Snapper, Scott B.
AU - Ramesh, Vijaya
PY - 2005/4/1
Y1 - 2005/4/1
N2 - The function of the NF2 tumor suppressor merlin has remained elusive despite increasing evidence for its role in actin cytoskeleton reorganization. The closely related ERM proteins (ezrin, radixin, and moesin) act as linkers between the cell membrane and cytoskeleton, and have also been implicated as active actin reorganizers. We report here that merlin and the ERMs can interact with and regulate N-WASP, a critical regulator of actin dynamics. Merlin and moesin were found to inhibit N-WASP-mediated actin assembly in vitro, a function that appears independent of their ability to bind actin. Furthermore, exogenous expression of a constitutively active ERM inhibits N-WASP-dependent Shigella tail formation, suggesting that the ERMs may function as inhibitors of N-WASP function in vivo. This novel function of merlin and the ERMs illustrates a mechanism by which these proteins directly exert their effects on actin reorganization and also provides new insight into N-WASP regulation.
AB - The function of the NF2 tumor suppressor merlin has remained elusive despite increasing evidence for its role in actin cytoskeleton reorganization. The closely related ERM proteins (ezrin, radixin, and moesin) act as linkers between the cell membrane and cytoskeleton, and have also been implicated as active actin reorganizers. We report here that merlin and the ERMs can interact with and regulate N-WASP, a critical regulator of actin dynamics. Merlin and moesin were found to inhibit N-WASP-mediated actin assembly in vitro, a function that appears independent of their ability to bind actin. Furthermore, exogenous expression of a constitutively active ERM inhibits N-WASP-dependent Shigella tail formation, suggesting that the ERMs may function as inhibitors of N-WASP function in vivo. This novel function of merlin and the ERMs illustrates a mechanism by which these proteins directly exert their effects on actin reorganization and also provides new insight into N-WASP regulation.
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UR - http://www.scopus.com/inward/citedby.url?scp=16844367763&partnerID=8YFLogxK
U2 - 10.1074/jbc.C400583200
DO - 10.1074/jbc.C400583200
M3 - Article
VL - 280
SP - 12517
EP - 12522
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 13
ER -