Direct signaling by the BMP type II receptor via the cytoskeletal regulator LIMK1

Foletta, Victoria, Lim, Mei Ann, Soosairaiah, Juliana, Kelly, April P., Stanley, Edouard G., Shannon, Mark, He, Wei, Das, Supratik, Massagué, Joan and Bernard, Ora 2003, Direct signaling by the BMP type II receptor via the cytoskeletal regulator LIMK1, Journal of cell biology, vol. 162, no. 6, pp. 1089-1098, doi: 10.1083/jcb.200212060.

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Title Direct signaling by the BMP type II receptor via the cytoskeletal regulator LIMK1
Author(s) Foletta, VictoriaORCID iD for Foletta, Victoria orcid.org/0000-0002-5209-6134
Lim, Mei Ann
Soosairaiah, Juliana
Kelly, April P.
Stanley, Edouard G.
Shannon, Mark
He, Wei
Das, Supratik
Massagué, Joan
Bernard, Ora
Journal name Journal of cell biology
Volume number 162
Issue number 6
Start page 1089
End page 1098
Total pages 11
Publisher Rockefeller University Press
Place of publication Birmingham, Ala.
Publication date 2003-09-15
ISSN 0021-9525
Summary Bone morphogenetic proteins (BMPs) regulate multiple cellular processes, including cell differentiation and migration. Their signals are transduced by the kinase receptors BMPR-I and BMPR-II, leading to Smad transcription factor activation via BMPR-I. LIM kinase (LIMK) 1 is a key regulator of actin dynamics as it phosphorylates and inactivates cofilin, an actin depolymerizing factor. During a search for LIMK1-interacting proteins, we isolated clones encompassing the tail region of BMPR-II. Although the BMPR-II tail is not involved in BMP signaling via Smad proteins, mutations truncating this domain are present in patients with primary pulmonary hypertension (PPH). Further analysis revealed that the interaction between LIMK1 and BMPR-II inhibited LIMK1's ability to phosphorylate cofilin, which could then be alleviated by addition of BMP4. A BMPR-II mutant containing the smallest COOH-terminal truncation described in PPH failed to bind or inhibit LIMK1. This study identifies the first function of the BMPR-II tail domain and suggests that the deregulation of actin dynamics may contribute to the etiology of PPH.
Language eng
DOI 10.1083/jcb.200212060
Indigenous content off
Field of Research 06 Biological Sciences
11 Medical and Health Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2003, The Rockefeller University Press
Persistent URL http://hdl.handle.net/10536/DRO/DU:30127361

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