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Myopodin Mediated Suppression of Prostate Cancer Cell Migration Involves Interaction with Zyxin
Author(s) -
Luo Jianhua,
Yu Yan Y
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a30-a
Subject(s) - motility , biology , regulator , mutant , metastasis , suppressor , microbiology and biotechnology , metastasis suppressor gene , cell migration , cancer research , prostate cancer , gene , cell , cancer , genetics
Myopodin was identified as a tumor suppressor gene that is frequently deleted in aggressive prostate cancer. Expression of myopodin protein suppresses both tumor growth and metastasis in vitro and in vivo. In the present study employing a yeast two‐hybrid system, we found that zyxin, a molecule known to regulate cell motility and migration, binds with myopodin with high affinity. The binding between zyxin and myopodin appears to be direct. Screening of a series of myopodin deletion mutants and peptide competition analyses revealed that myopodin is bound by zyxin at a site located within the sequence of the 19 amino acids at the myopodin C‐terminus. Importantly, this is the same region where the tumor suppressor activity of myopodin is located. The motility and invasion suppression activity of myopodin were significantly weakened in myopodin mutants lacking this sequence. Thus our studies suggest that zyxin may be a critical functional regulator of myopodin.