کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2050430 1074170 2008 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
The mammalian CHORD-containing protein melusin is a stress response protein interacting with Hsp90 and Sgt1
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
The mammalian CHORD-containing protein melusin is a stress response protein interacting with Hsp90 and Sgt1
چکیده انگلیسی

Melusin is a mammalian muscle specific CHORD containing protein capable of activating signal transduction pathways leading to cardiomyocytes hypertrophy in response to mechanical stress. To define melusin function we searched for molecular partners possibly involved in melusin dependent signal transduction. Here we show that melusin and heat shock proteins are co-regulated. Moreover, melusin directly binds to Hsp90, a ubiquitous chaperone involved in regulating several signaling pathways. In addition, melusin interacts with Sgt1, an Hsp90 binding molecule. Melusin does not behave as an Hsp90 substrate but rather as a chaperone capable to protect citrate synthase from heat induced aggregation. These results describe melusin as a new component of the Hsp90 chaperone machinery.Structured summaryMINT-6538515:melusin (Q9R000)physically interacts (MI:0218) with Hsp90 (P07901) by anti bait co-immunoprecipitation (MI:0006)MINT-6538566, MINT-6538556:Hsp90 (P07901) physically interacts (MI:0218) with melusin (Q9R000) by cross-linking studies (MI:0030)MINT-6538524:melusin (Q9R000) physically interacts (MI:0218) with Sgt1 (Q9CS74) by anti tag co-immunoprecipitation (MI:0007)MINT-6538595:Hsp90 (P07901) physically interacts (MI:0218) with melusin (Q9R000) by enzyme linked immunosorbent assay (MI:0411)MINT-6538543:melusin (Q9R000) physically interacts (MI:0218) with Sgt1 (Q9CS74) by anti bait co-immunoprecipitation (MI:0006)MINT-6538580: melusin (Q9R000) physically interacts (MI:0218) with Hsp90 (P07901) by surface plasmon resonance (MI:0107)

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 582, Issue 13, 11 June 2008, Pages 1788–1794
نویسندگان
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