{"id":3491,"date":"2016-04-13T09:52:32","date_gmt":"2016-04-13T00:52:32","guid":{"rendered":"https:\/\/www.peptide.co.jp\/en\/?p=3491"},"modified":"2023-08-29T10:17:39","modified_gmt":"2023-08-29T01:17:39","slug":"3108","status":"publish","type":"post","link":"https:\/\/www.peptide.co.jp\/en\/new-product\/3108.html","title":{"rendered":"Phopsho Ubiquitin: [Ser(PO3<\/sub>H2<\/sub>)65<\/sup>]-Ubiquitin"},"content":{"rendered":"

In 2014, Koyano et al<\/i>.1)<\/sup> and other groups2)-4)<\/sup> reported a novel function of ubiquitin, that [Ser(PO3<\/sub>H2<\/sub>)65<\/sup>]-ubiquitin (phosphorylated ubiquitin at Ser65<\/sup>) is clarified to be an essential player in mitochondrial quality control. PINK1 (PTEN-induced protein kinase 1) phosphorylates ubiquitin at Ser65<\/sup>, as well as Parkin (E3 ubiquitin ligase) at the similar Ser residue in its ubiquitin-like domain upon depolarization of mitochondrial membrane (mitochondria damage), which follows the activation of latent Parkin E3 by retrieving the catalytic cysteine from autoinhibition.<\/p>\n

\"phosphoUb_en\"<\/p>\n

After this initial observation, research in relation to phosphorylation of ubiquitin has been increasing tremendously, including: i) activation mechanism of Parkin by [Ser(PO3<\/sub>H2<\/sub>)65<\/sup>]-ubiquitin by crystallographic analysis using Pediculus humanus Parkin5)<\/sup>, ii) disposal of damaged mitochondria through mitophagic pathway where [Ser(PO3<\/sub>H2<\/sub>)65<\/sup>]-ubiquitin, phosphorylated by PINK1, is involved in inducing autophagy receptor recruitment6)<\/sup><\/p>\n

These experimental results imply that [Ser(PO3<\/sub>H2<\/sub>)65<\/sup>]-ubiquitin may shed light on the research of Parkinson\u2019s disease which is associated with mitochondrial dysfunction.<\/p>\n

\u3000<\/p>\n\n\n\n\n\n
Code<\/td>\nCompound<\/td>\nQuantity<\/td>\n<\/tr>\n
4486-v <\/a><\/td>\n[Ser(PO3<\/sub>H2<\/sub>)65<\/sup>]-Ubiquitin<\/td>\n50 \u03bcg vial<\/td>\n<\/tr>\n
3207-v <\/a><\/td>\nUbiquitin Aldehyde<\/td>\n50 \u03bcg vial<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n

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Feel free to contact us if you have any questions.<\/a><\/Div><\/p>\n
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  1. Nature<\/i>, 510<\/B>, 162 (2014). DOI: 10.1038\/nature13392<\/a> (Original)<\/i><\/li>\n
  2. J. Cell Biol.<\/i>, 205<\/B>, 143 (2014). DOI: 10.1083\/jcb.201402104<\/a> (Original)<\/i><\/li>\n
  3. Biochem. J.<\/i>, 460<\/B>, 127 (2014). DOI: 10.1042\/BJ20140334<\/a> (Original)<\/i><\/li>\n
  4. Mol. Cell<\/i>, 56<\/B>, 360 (2014). DOI: 10.1016\/j.molcel.2014.09.007<\/a> (Original)<\/i><\/li>\n
  5. Nature<\/i>, 524<\/B>, 370 (2015). DOI: 10.1038\/nature14879<\/a> (Role in Parkin Activation)<\/i><\/li>\n
  6. Nature<\/i>, 524<\/B>, 309 (2015). DOI: 10.1038\/nature14893<\/a> (Role in Mitophagy)<\/i><\/li>\n

    \u3000
    \n\u3000<\/p>\n","protected":false},"excerpt":{"rendered":"

    In 2014, Koyano et al.1) and other groups2)-4) reported a novel function of ubiquitin, that [Ser(PO3H2)65]-ubiquitin (phosphorylated ubiquitin at Ser65) is clarified to be an essential player in mitochondrial quality control. PINK1 (PTEN-induced protein kinase 1) phosphorylates ubiquitin at Ser65, as well as Parkin (E3 ubiquitin ligase) at the similar Ser residue in its ubiquitin-like domain upon depolarization of mitochondrial membrane (mitochondria damage), which follows the activation of latent Parkin E3 by retrieving the catalytic cysteine from autoinhibition. After this initial observation, research in relation to phosphorylation of ubiquitin has been increasing tremendously, including: i) activation mechanism of Parkin by [Ser(PO3H2)65]-ubiquitin by crystallographic analysis using Pediculus humanus Parkin5), ii) disposal […]<\/p>\n","protected":false},"author":2,"featured_media":0,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[2],"tags":[],"class_list":["post-3491","post","type-post","status-publish","format-standard","hentry","category-new-product"],"acf":[],"_links":{"self":[{"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/posts\/3491","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/users\/2"}],"replies":[{"embeddable":true,"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/comments?post=3491"}],"version-history":[{"count":6,"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/posts\/3491\/revisions"}],"predecessor-version":[{"id":4929,"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/posts\/3491\/revisions\/4929"}],"wp:attachment":[{"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/media?parent=3491"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/categories?post=3491"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/tags?post=3491"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}