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Heterodimerization is mainly responsible for the dominant negative activity of amino‐terminally truncated rat androgen receptor forms
Author(s) -
Ikonen T.,
Palvimo J.J.,
Jänne O.A.
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00701-7
Subject(s) - androgen receptor , terminally ill , receptor , chemistry , microbiology and biotechnology , biology , biochemistry , genetics , medicine , cancer , prostate cancer , palliative care , nursing
Rat androgen receptor (rAR) mutants devoid of the amino‐terminal transactivation domain are able to behave as dominant negative regulators of wild‐type rAR. To address the underlying mechanisms of the trans ‐dominant negative action, we have examined the roles of the DNA‐binding domain (DBD) and the ligand‐binding domain (LBD) in this process. Transactivation experiments in CV‐1 cells complemented by electrophoretic mobility shift assays revealed that the dominant negative receptor forms repress the function of wild‐type rAR mainly through heterodimer formation, rather than through competition for binding to cognate DNA elements. Heterodimerization of receptor forms containing LBDs may take place even in the absence of specific DNA binding.