کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2131700 1086655 2008 14 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Spatial control of protein phosphatase 2A (de)methylation
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی تحقیقات سرطان
پیش نمایش صفحه اول مقاله
Spatial control of protein phosphatase 2A (de)methylation
چکیده انگلیسی

Reversible methylation of the protein phosphatase 2A catalytic subunit (PP2AC1) is an important regulatory mechanism playing a crucial role in the selective recruitment of regulatory B subunits. Here, we investigated the subcellular localization of leucine carboxyl methyltransferase (LCMT1) and protein phosphatase methylesterase (PME-1), the two enzymes catalyzing this process. The results show that PME-1 is predominantly localized in the nucleus and harbors a functional nuclear localization signal, whereas LCMT1 is underrepresented in the nucleus and mainly localizes to the cytoplasm, Golgi region and late endosomes. Indirect immunofluorescence with methylation-sensitive anti-PP2AC antibodies revealed a good correlation with the methylation status of PP2AC, demethylated PP2AC being substantially nuclear. Throughout mitosis, demethylated PP2AC is associated with the mitotic spindle and during cytokinesis with the cleavage furrow. Overexpression of PME-1, but not of an inactive mutant, results in increased demethylation of PP2AC in the nucleus, whereas overexpression of a cytoplasmic PME-1 mutant lacking the NLS results in increased demethylation in the cytoplasm—in all cases, however, without any obvious functional consequences. PME-1 associates with an inactive PP2A population, regardless of its esterase activity or localization. We propose that stabilization of this inactive, nuclear PP2A pool is a major in vivo function of PME-1.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Experimental Cell Research - Volume 314, Issue 1, 1 January 2008, Pages 68–81
نویسندگان
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