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

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    Author
    Foletta, VC; Lim, MA; Soosairaiah, J; Kelly, AP; Stanley, EG; Shannon, M; He, W; Das, S; Massague, J; Bernard, O
    Date
    2003-09-15
    Source Title
    The Journal of Cell Biology
    Publisher
    ROCKEFELLER UNIV PRESS
    University of Melbourne Author/s
    Stanley, Edouard
    Affiliation
    Paediatrics (RCH)
    Metadata
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    Document Type
    Journal Article
    Citations
    Foletta, V. C., Lim, M. A., Soosairaiah, J., Kelly, A. P., Stanley, E. G., Shannon, M., He, W., Das, S., Massague, J. & Bernard, O. (2003). Direct signaling by the BMP type II receptor via the cytoskeletal regulator LIMK1. JOURNAL OF CELL BIOLOGY, 162 (6), pp.1089-1098. https://doi.org/10.1083/jcb.200212060.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/256757
    DOI
    10.1083/jcb.200212060
    Abstract
    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.

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