DOI: 10.1073/pnas.1918462117
论文题名: Distinct activities of Scrib module proteins organize epithelial polarity
作者: Khoury M.J. ; Bilder D.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2020
卷: 117, 期: 21 语种: 英语
英文关键词: Drosophila
; Epithelia
; Par complex
; Polarity
; Scrib module
Scopus关键词: cell protein
; phospholipid
; protein kinase C
; Scrib module protein
; unclassified drug
; aPKC protein, Drosophila
; dlg1 protein, Drosophila
; Drosophila protein
; l(2)gl protein, Drosophila
; membrane protein
; protein kinase C
; Scrib protein, Drosophila
; tumor suppressor protein
; Article
; cell membrane
; cell polarity
; controlled study
; Drosophila
; epithelium cell
; larva
; nonhuman
; palmitoylation
; polarization
; priority journal
; protein localization
; protein protein interaction
; animal
; cell polarity
; cytology
; Drosophila
; epithelium
; female
; ovary follicle
; physiology
; Animals
; Cell Polarity
; Drosophila
; Drosophila Proteins
; Epithelial Cells
; Epithelium
; Female
; Membrane Proteins
; Ovarian Follicle
; Protein Kinase C
; Tumor Suppressor Proteins
英文摘要: A polarized architecture is central to both epithelial structure and function. In many cells, polarity involves mutual antagonism between the Par complex and the Scribble (Scrib) module. While molecular mechanisms underlying Par-mediated apical determination are well-understood, how Scrib module proteins specify the basolateral domain remains unknown. Here, we demonstrate dependent and independent activities of Scrib, Discs-large (Dlg), and Lethal giant larvae (Lgl) using the Drosophila follicle epithelium. Our data support a linear hierarchy for localization, but rule out previously proposed protein-protein interactions as essential for polarization. Cortical recruitment of Scrib does not require palmitoylation or polar phospholipid binding but instead an independent cortically stabilizing activity of Dlg. Scrib and Dlg do not directly antagonize atypical protein kinase C (aPKC), but may instead restrict aPKC localization by enabling the aPKC-inhibiting activity of Lgl. Importantly, while Scrib, Dlg, and Lgl are each required, all three together are not sufficient to antagonize the Par complex. Our data demonstrate previously unappreciated diversity of function within the Scrib module and begin to define the elusive molecular functions of Scrib and Dlg. © 2020 National Academy of Sciences. All rights reserved. Citation statistics:
资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163463
Appears in Collections: 气候变化与战略
There are no files associated with this item.
作者单位: Khoury, M.J., Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, United States; Bilder, D., Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, United States
Recommended Citation:
Khoury M.J.,Bilder D.. Distinct activities of Scrib module proteins organize epithelial polarity[J]. Proceedings of the National Academy of Sciences of the United States of America,2020-01-01,117(21)