Posttranslational Modifications in Innate Immunity
نویسندگان
چکیده
منابع مشابه
Posttranslational modifications in innate immunity.
Taking into account that a large number of nascent gene translation products are subject to limited proteolytic processing, proteolysis is one of the most common PTMs and due to its irreversible nature needs to be very precisely controlled on multiple levels. Since PTMs play a key role in fundamental cellular processes, including the immune response, it is no surprise that these reactions are t...
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TGF-β activated kinase 1 (TAK1) is a critical signaling hub responsible for translating antigen binding signals to immune receptors for the activation of the AP-1 and NF-κB master transcriptional programs. Despite its importance, known substrates of TAK1 are limited to kinases of the MAPK and IKK families and include no direct effectors of biochemical processes. Here, we identify over 200 subst...
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P ho sp ho ry la ti o n N-Terminal: S6, S9, S15, T18, S20 ATM, DNAPK, • CK1 ERKs, ATR, p38 • kinase, mTOR, Chk1/Chk2, JNK, MAPKAP2, Hipk4 Activated by DNA damage, UV light, ionizing radiation, replicative senes• cence, or phosphatidylcholines. N-terminal phosphorylation causes p53 stabilization by inhibiting the p53• MDM2 interaction. Knockin mice carrying separate analogs to human Ser18/ • Ser...
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Posttranslational modifications of proteins are key effectors of enzyme activity, protein interactions, targeting, and turnover rate, but despite their importance, they are still poorly understood in plants. Although numerous reports have revealed the regulatory role of protein phosphorylation in photosynthesis, various other protein modifications have been identified in chloroplasts only recen...
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Tissue factor (TF), a membrane protein, is an initiator of blood coagulation in vivo. In this review we discuss how posttranslational modifications affect activity and other properties of TF. Glycosylation of the extracellular domain and the composition of carbohydrates at three glycosylation sites have an influence on TF activity in the extrinsic FXase by increasing the rate of FX proteolysis....
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ژورنال
عنوان ژورنال: Journal of Innate Immunity
سال: 2012
ISSN: 1662-8128,1662-811X
DOI: 10.1159/000336327