مورد إلكتروني
The amphipathic helices of Arfrp1 and Arl14 are sufficient to determine subcellular localizations
العنوان: | The amphipathic helices of Arfrp1 and Arl14 are sufficient to determine subcellular localizations |
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بيانات النشر: | 2020 |
تفاصيل مُضافة: | Yang, Feng Li, Tiantian Peng, Ziqing Liu, Yang Guo, Yusong |
نوع الوثيقة: | Electronic Resource |
مستخلص: | The subcellular localization of Arf family proteins is generally thought to be determined by their corresponding guanine nucleotide exchange factors (GEFs). By promoting GTP binding, GEFs induce conformational changes of Arf proteins exposing their N-terminal amphipathic helices, which then insert into the membranes to stabilize the membrane association process. Here, we found the N-terminal amphipathic motifs of the Golgi-localized Arf family protein, Arfrp1, and the endosome- and plasma membrane-localized Arf family protein, Arl14, play critical roles in spatial determination. Exchanging the amphipathic helix motifs between these two Arf proteins causes the switch of their localizations. Moreover, the amphipathic helices of Arfrp1 and Arl14 are sufficient for cytosolic proteins to be localized into a specific cellular compartment. The spatial determination mediated by the Arfrp1 helix requires its binding partner Sys1. In addition, the residues that are required for the acetylation of the Arfrp1 helix and the myristoylation of the Arl14 helix are important for the specific subcellular localization. Interestingly, Arfrp1 and Arl14 are recruited to their specific cellular compartments independent of GTP binding. Our results demonstrate that the amphipathic motifs of Arfrp1 and Arl14 are sufficient for determining specific subcellular localizations in a GTP-independent manner, suggesting the membrane association and activation of some Arf proteins are uncoupled. |
مصطلحات الفهرس: | ARF, Article |
URL: | |
الإتاحة: | Open access content. Open access content |
ملاحظة: | English |
أرقام أخرى: | HNK oai:repository.hkust.edu.hk:1783.1-105344 Journal of Biological Chemistry, v. 295, (49), December 2020, p. 16643-16654 0021-9258 https://doi.org/10.1074/jbc.RA120.014999 1331250358 |
المصدر المساهم: | HONG KONG UNIV OF SCI & TECH, THE From OAIster®, provided by the OCLC Cooperative. |
رقم الأكسشن: | edsoai.on1331250358 |
قاعدة البيانات: | OAIster |
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