Repository logo
  • English
  • 中文
Log In
Have you forgotten your password?
  1. Home
  2. College of Medicine / 醫學院
  3. Molecular Medicine / 分子醫學研究所
  4. BTB-kelch蛋白KLEIP在Golgi complex之特性分析與功能探討
 
  • Details

BTB-kelch蛋白KLEIP在Golgi complex之特性分析與功能探討

Characterization of the subcellular localizations of KLEIP and its function in vesicular trafficking

Date Issued
2007
Date
2007
Author(s)
Yuan, Wei-Chien
DOI
en-US
URI
http://ntur.lib.ntu.edu.tw//handle/246246/51376
Abstract
KLEIP (kelch-like ECT2 interacting protein) contains one BTB/POZ domain, one BACK and six kelch repeats. Previous study in our laboratory demonstrated that KLEIP, DAPK, and Cul3 form an E3 ubiquitin ligase complex to regulate the stability of DAPK by mediating its ubiquitination. In this thesis, we identify the subcellular localizations of KLEIP. KLEIP is present in both cell-cell contact and Golgi apparatus. The Golgi localization of KLEIP was further confirmed by the cofractionation of KLEIP with Golgi proteins. The recruitment of KLEIP to Golgi is dependent on actin polymerization and the activity of Arf1, which is involved in actin polymerization at Golgi. In line with its Golgi residence, KLEIP is crucial for maintaining Golgi architecture, as the ultrastructure of Golgi complex is fragmented with shortened and swollen cisternae in KLEIP knockdown cells. In addition, knockdown of KLEIP leads to the delay of post-Golgi transport to plasma membrane without affecting retrograde traffiking from plasma membrane to Golgi. In addition to localizing in Golgi, KLEIP can also be recruited to PML nuclear body when PML or SUMO is overexpressed, suggesting that KLEIP may be modified or associated with SUMO. Together, this study uncovers a role of KLEIP in the anterograde trafficking process. We hypothesize that KLEIP affects an actin-dependent trafficking step. Furthermore, the existence of KLEIP in multiple subcellular compartments implies its involvement in trafficking-unrelated cellular functions.
Subjects
運輸
類泛素化
KLEIP
Golgi
trafficking
SUMO
Type
other
File(s)
Loading...
Thumbnail Image
Name

ntu-96-R94448003-1.pdf

Size

23.31 KB

Format

Adobe PDF

Checksum

(MD5):84d9befcef312f1aad5849851c450feb

臺大位居世界頂尖大學之列,為永久珍藏及向國際展現本校豐碩的研究成果及學術能量,圖書館整合機構典藏(NTUR)與學術庫(AH)不同功能平台,成為臺大學術典藏NTU scholars。期能整合研究能量、促進交流合作、保存學術產出、推廣研究成果。

To permanently archive and promote researcher profiles and scholarly works, Library integrates the services of “NTU Repository” with “Academic Hub” to form NTU Scholars.

總館學科館員 (Main Library)
醫學圖書館學科館員 (Medical Library)
社會科學院辜振甫紀念圖書館學科館員 (Social Sciences Library)

開放取用是從使用者角度提升資訊取用性的社會運動,應用在學術研究上是透過將研究著作公開供使用者自由取閱,以促進學術傳播及因應期刊訂購費用逐年攀升。同時可加速研究發展、提升研究影響力,NTU Scholars即為本校的開放取用典藏(OA Archive)平台。(點選深入了解OA)

  • 請確認所上傳的全文是原創的內容,若該文件包含部分內容的版權非匯入者所有,或由第三方贊助與合作完成,請確認該版權所有者及第三方同意提供此授權。
    Please represent that the submission is your original work, and that you have the right to grant the rights to upload.
  • 若欲上傳已出版的全文電子檔,可使用Open policy finder網站查詢,以確認出版單位之版權政策。
    Please use Open policy finder to find a summary of permissions that are normally given as part of each publisher's copyright transfer agreement.
  • 網站簡介 (Quickstart Guide)
  • 使用手冊 (Instruction Manual)
  • 線上預約服務 (Booking Service)
  • 方案一:臺灣大學計算機中心帳號登入
    (With C&INC Email Account)
  • 方案二:ORCID帳號登入 (With ORCID)
  • 方案一:定期更新ORCID者,以ID匯入 (Search for identifier (ORCID))
  • 方案二:自行建檔 (Default mode Submission)
  • 方案三:學科館員協助匯入 (Email worklist to subject librarians)

Built with DSpace-CRIS software - Extension maintained and optimized by 4Science