scholarly journals The Strip-Hippo Pathway Regulates Synaptic Terminal Formation by Modulating Actin Organization at the Drosophila Neuromuscular Synapses

Cell Reports ◽  
2016 ◽  
Vol 16 (9) ◽  
pp. 2289-2297 ◽  
Author(s):  
Chisako Sakuma ◽  
Yoshie Saito ◽  
Tomoki Umehara ◽  
Keisuke Kamimura ◽  
Nobuaki Maeda ◽  
...  
Keyword(s):  
Hippo Pathway ◽  
Synaptic Terminal ◽  
Actin Organization ◽  
Neuromuscular Synapses

scholarly journals Modulating F-actin organization induces organ growth by affecting the Hippo pathway

2011 ◽  
Vol 30 (12) ◽  
pp. 2325-2335 ◽  
Author(s):  
Leticia Sansores-Garcia ◽  
Wouter Bossuyt ◽  
Ken-Ichi Wada ◽  
Shigenobu Yonemura ◽  
Chunyao Tao ◽  
...  
Keyword(s):  
Hippo Pathway ◽  
Organ Growth ◽  
Actin Organization ◽  
The Hippo Pathway

scholarly journals Angiomotin regulates budding and spread of Ebola virus

2020 ◽  
Vol 295 (25) ◽  
pp. 8596-8601
Author(s):  
Ziying Han ◽  
Gordon Ruthel ◽  
Shantoshini Dash ◽  
Corbett T. Berry ◽  
Bruce D. Freedman ◽  
...  
Keyword(s):  
Matrix Protein ◽  
Ebola Virus ◽  
Hippo Pathway ◽  
Adaptor Protein ◽  
Actin Dynamics ◽  
Hippo Signaling ◽  
Dependent Manner ◽  
Host Proteins ◽  
Ww Domain ◽  
Actin Organization

The Ebola virus (EBOV) VP40 matrix protein (eVP40) orchestrates assembly and budding of virions in part by hijacking select WW-domain–bearing host proteins via its PPxY late (L)-domain motif. Angiomotin (Amot) is a multifunctional PPxY-containing adaptor protein that regulates angiogenesis, actin dynamics, and cell migration/motility. Amot also regulates the Hippo signaling pathway via interactions with the WW-domain–containing Hippo effector protein Yes-associated protein (YAP). In this report, we demonstrate that endogenous Amot is crucial for positively regulating egress of eVP40 virus-like particles (VLPs) and for egress and spread of authentic EBOV. Mechanistically, we show that ectopic YAP expression inhibits eVP40 VLP egress and that Amot co-expression rescues budding of eVP40 VLPs in a dose-dependent and PPxY-dependent manner. Moreover, results obtained with confocal and total internal reflection fluorescence microscopy suggested that Amot's role in actin organization and dynamics also contributes to promoting eVP40-mediated egress. In summary, these findings reveal a functional and competitive interplay between virus and host proteins involving the multifunctional PPxY-containing adaptor Amot, which regulates both the Hippo pathway and actin dynamics. We propose that our results have wide-ranging implications for understanding the biology and pathology of EBOV infections.

scholarly journals WTS-1/LATS regulates endocytic recycling by restraining F-actin assembly in a synergistic manner

2021 ◽  
Author(s):  
Hanchong Zhang ◽  
Zihang Cheng ◽  
Wenbo Li ◽  
Jie Hu ◽  
Linyue Zhao ◽  
...  
Keyword(s):  
Actin Polymerization ◽  
Hippo Pathway ◽  
Actin Assembly ◽  
Core Component ◽  
Endocytic Recycling ◽  
Actin Organization ◽  
C Elegans ◽  
The Hippo Pathway ◽  
Homeostatic Mechanisms

The disruption of endosomal actin architecture negatively affects endocytic recycling. However, the underlying homeostatic mechanisms that regulate actin organization during recycling remain unclear. In this study, we identified a synergistic endosomal actin assembly restricting mechanism in C. elegans involving WTS-1/LATS kinase, which is a core component of the Hippo pathway. WTS-1 resides on the sorting endosomes and colocalizes with the actin polymerization regulator PTRN-1/CAMSAPs. We observed an increase in PTRN-1-labeled structures in WTS-1-deficient cells, indicating that WTS-1 can limit the endosomal localization of PTRN-1. Accordingly, the actin overaccumulation phenotype in WTS-1-depleted cells was mitigated by the associated PTRN-1 loss. We further demonstrated that recycling defects and actin overaccumulation in WTS-1-deficient cells were reduced by the overexpression of constitutively active UNC-60A/cofilin(S3A), which aligns with the role of LATS as a positive regulator of cofilin activity. Altogether, our data confirmed previous findings, and we proposed an additional model: WTS-1 acts alongside the UNC-60A/cofilin-mediated actin disassembly to restrict the assembly of endosomal F-actin by curbing PTRN-1 dwelling on endosomes, preserving recycling transport.

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