Role of p21-activated kinase in cell polarity and directional mesendoderm migration in theXenopusgastrula

2009 ◽  
Vol 238 (7) ◽  
pp. 1709-1726 ◽  
Author(s):  
Martina Nagel ◽  
Olivia Luu ◽  
Nicolas Bisson ◽  
Bojan Macanovic ◽  
Tom Moss ◽  
...  
2006 ◽  
Vol 281 (45) ◽  
pp. 34716-34724 ◽  
Author(s):  
Qing-Fen Li ◽  
Amy M. Spinelli ◽  
Ruping Wang ◽  
Yana Anfinogenova ◽  
Harold A. Singer ◽  
...  

2008 ◽  
Vol 319 (2) ◽  
pp. 482
Author(s):  
Molly J. Ahrens ◽  
Andrew T. Dudley
Keyword(s):  

Development ◽  
2021 ◽  
pp. dev.196956
Author(s):  
Juan Lu ◽  
Wei Dong ◽  
Yan Tao ◽  
Yang Hong

Discs large (Dlg) is an essential polarity protein and a tumor suppressor originally characterized in Drosophila but is also well conserved in vertebrates. Like the majority of polarity proteins, plasma membrane (PM)/cortical localization of Dlg is required for its function in polarity and tumorigenesis, but the exact mechanisms targeting Dlg to PM remain to be fully elucidated. Here we show that, similar to the recently discovered polybasic polarity proteins such as Lgl and aPKC, Dlg also contains a positively charged polybasic domain that electrostatically binds the PM phosphoinositides PI4P and PI(4,5)P2. Electrostatic targeting by the polybasic domain contributes significantly to the PM localization of Dlg in follicular and early embryonic epithelial cells, and is crucial for Dlg to regulate both polarity and tumorigenesis. The electrostatic PM targeting of Dlg is controlled by a potential phosphorylation-dependent allosteric regulation of its polybasic domain, and is specifically enhanced by the interactions between Dlg and another basolateral polarity protein and tumor suppressor Scrib. Our studies highlight an increasingly significant role of electrostatic PM targeting of polarity proteins in regulating cell polarity.


2020 ◽  
Vol 40 (1) ◽  
Author(s):  
Wanli Ma ◽  
Xiaohe Wang ◽  
Chunhui Wang ◽  
Mingzhi Gong ◽  
Peng Ren

Abstract Osteoarthritis is mainly caused by a degenerative joint disorder, which is characterized by the gradual degradation of articular cartilage and synovial inflammation. The chondrocyte, the unique resident cell type of articular cartilage, is crucial for the development of osteoarthritis. Previous studies revealed that P21-activated kinase-1 (PAK1) was responsible for the initiation of inflammation. The purpose of the present study was to determine the potential role of PAK1 in osteoarthritis. The level of PAK1 expression was measured by Western blot and quantitative real-time PCR in articular cartilage from osteoarthritis model rats and patients with osteoarthritis. In addition, the functional role of aberrant PAK1 expression was detected in the chondrocytes. We found that the expression of PAK1 was significantly increased in chondrocytes treated with osteoarthritis-related factors. Increased expression of PAK1 was also observed in knee articular cartilage samples from patients with osteoarthritis and osteoarthritis model rats. PAK1 was found to inhibit chondrocytes proliferation and to promote the production of inflammatory cytokines in cartilages chondrocytes. Furthermore, we found that PAK1 modulated the production of extracellular matrix and cartilage degrading enzymes in chondrocytes. Results of the present studies demonstrated that PAK1 might play an important role in the pathogenesis of osteoarthritis.


2011 ◽  
Vol 90 (2-3) ◽  
pp. 198-204 ◽  
Author(s):  
James Monypenny ◽  
Hsiu-Chuan Chou ◽  
Inmaculada Bañón-Rodríguez ◽  
Adrian J. Thrasher ◽  
Inés M. Antón ◽  
...  
Keyword(s):  

2010 ◽  
Author(s):  
Nina Holderness ◽  
Howard Donninger ◽  
Michael J. Birrer ◽  
Virna Leaner
Keyword(s):  

2002 ◽  
Vol 383 (10) ◽  
pp. 1475-1480 ◽  
Author(s):  
M. Bagnat ◽  
K. Simons

Abstract Cellular membranes contain many types and species of lipids. One of the most important functional consequences of this heterogeneity is the existence of microdomains within the plane of the membrane. Sphingolipid acyl chains have the ability of forming tightly packed platforms together with sterols. These platforms or lipid rafts constitute segregation and sorting devices into which proteins specifically associate. In budding yeast, Saccharomyces cerevisiae, lipid rafts serve as sorting platforms for proteins destined to the cell surface. The segregation capacity of rafts also provides the basis for the polarization of proteins at the cell surface during mating. Here we discuss some recent findings that stress the role of lipid rafts as key players in yeast protein sorting and cell polarity.


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