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J Biol Chem, Vol. 273, Issue 6, 3117-3120, February 6, 1998
From the Division of Molecular Medicine, Department of Internal
Medicine, and Research Center for Cardiovascular Diseases, Institute of
Molecular Medicine for the Prevention of Human Diseases, The
University of Texas-Houston Health Science Center,
Houston, Texas 77030
PML, a RING finger protein with tumor suppressor
activity, has been implicated in the pathogenesis of acute
promyelocytic leukemia that arises following a reciprocal chromosomal
translocation that fuses the PML gene with the retinoic acid receptor
(RAR) gene. Immunocytochemical analysis has demonstrated that
PML is co-localized with a novel ubiquitin-like protein in the nuclear bodies, which could be disrupted by the PML-RAR fusion protein. The
physical nature of this co-localization is unknown. Using a COS cell
expression system, we show that PML is covalently modified by all three
members of the sentrin family of ubiquitin-like proteins. Covalent
modification of PML requires the conserved Gly residue near the C
termini of sentrin proteins. Sentrinization of PML is highly specific
because neither NEDD8 nor ubiquitin could modify PML. Similar
specificity is also observed for the covalent modification of RanGAP1
by the sentrin member of ubiquitin-like proteins. These observations
highlight the fine substrate specificity of the sentrinization pathway.
In acute promyelocytic leukemia, two forms of PML-RAR fusion
proteins have been reported. Remarkably, both forms of PML-RAR
fusion proteins could not be sentrinized. Thus differential sentrinization of PML and PML-RAR could play an important role in
regulating the biological function of PML and in the pathogenesis of
acute promyelocytic leukemia.
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