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
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
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