کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
3056393 1186565 2009 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Ataxin-2 associates with rough endoplasmic reticulum
موضوعات مرتبط
علوم زیستی و بیوفناوری علم عصب شناسی عصب شناسی
پیش نمایش صفحه اول مقاله
Ataxin-2 associates with rough endoplasmic reticulum
چکیده انگلیسی

Ataxin-2 is a novel protein, normally with a domain of 22 consecutive glutamine (Q) residues, which may expand beyond a threshold of (Q)32, causing a neurodegenerative disease named Spinocerebellar ataxia type 2 (SCA2). To obtain clues about the functions of ataxin-2, we used fluorescence microscopy and centrifugation fractionation analyses. Immunocytochemical detection in non-neuronal and neuronal cells showed endogenous and transfected ataxin-2 distributed throughout the cytoplasm, with perinuclear preference and a granular appearance. Triple-labelling and confocal microscopy demonstrated co-localisation with the endoplasmic reticulum (ER) markers calreticulin, calnexin and CFP-ER. The pathogenic form of ataxin-2 with an expanded polyQ domain showed the same distribution pattern. Subcellular fractionation of mouse brain homogenates showed endogenous ataxin-2 associated with rough ER (rER) membranes, in a manner dependent on RNA, salt and phosphorylation. Our data are in agreement with recent findings that ataxin-2 directly interacts with poly(A)-binding protein (PABP), thus associating with polyribosomes under normal conditions and being recruited to stress granules under environmental stress. These data, in conjunction with the presence of Lsm domains within ataxin-2, suggest that ataxin-2 is involved in the processing of mRNA and/or the regulation of translation.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Experimental Neurology - Volume 215, Issue 1, January 2009, Pages 110–118
نویسندگان
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