scholarly journals Ptc1 and Ptc2 Transcripts Provide Distinct Readouts of Hedgehog Signaling Activity during Chick Embryogenesis

2001 ◽  
Vol 239 (1) ◽  
pp. 15-29 ◽  
Author(s):  
Richard V. Pearse ◽  
Kyle J. Vogan ◽  
Clifford J. Tabin
2020 ◽  
Vol 387 ◽  
pp. 114853 ◽  
Author(s):  
Shen Jiayuan ◽  
Yan Junyan ◽  
Wei Xiangzhen ◽  
Liu Zuping ◽  
Ni Jian ◽  
...  

2019 ◽  
Vol 381 (2) ◽  
pp. 311-322 ◽  
Author(s):  
Verónica Rojo-León ◽  
Celina García ◽  
Concepción Valencia ◽  
Marco-Antonio Méndez ◽  
Christopher Wood ◽  
...  

PLoS Biology ◽  
2016 ◽  
Vol 14 (6) ◽  
pp. e1002481 ◽  
Author(s):  
Shuangxi Li ◽  
Shuang Li ◽  
Yuhong Han ◽  
Chao Tong ◽  
Bing Wang ◽  
...  

2007 ◽  
Vol 41 (12) ◽  
pp. 1238-1239 ◽  
Author(s):  
Bayasi Guleng ◽  
Keisuke Tateishi ◽  
Miki Ohta ◽  
Yoshinari Asaoka ◽  
Amarsanaa Jazag ◽  
...  

Cells ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 2138
Author(s):  
Jie Zhang ◽  
Zulong Liu ◽  
Jianhang Jia

The seven-transmembrane protein, Smoothened (SMO), has shown to be critical for the hedgehog (HH) signal transduction on the cell membrane (and the cilium in vertebrates). SMO is subjected to multiple types of post-translational regulations, including phosphorylation, ubiquitination, and sumoylation, which alter SMO intracellular trafficking and cell surface accumulation. Recently, SMO is also shown to be regulated by small molecules, such as oxysterol, cholesterol, and phospholipid. The activity of SMO must be very well balanced by these different mechanisms in vivo because the malfunction of SMO will not only cause developmental defects in early stages, but also induce cancers in late stages. Here, we discuss the activation and inactivation of SMO by different mechanisms to better understand how SMO is regulated by the graded HH signaling activity that eventually governs distinct development outcomes.


2020 ◽  
Vol 220 (2) ◽  
Author(s):  
Min Liu ◽  
Aiguo Liu ◽  
Jie Wang ◽  
Yansong Zhang ◽  
Yajuan Li ◽  
...  

Hedgehog (Hh) signaling is essential for embryonic development and adult homeostasis. How its signaling activity is fine-tuned in response to fluctuated Hh gradient is less known. Here, we identify protein phosphatase V (PpV), the catalytic subunit of protein phosphatase 6, as a homeostatic regulator of Hh signaling. PpV is genetically upstream of widerborst (wdb), which encodes a regulatory subunit of PP2A that modulates high-level Hh signaling. We show that PpV negatively regulates Wdb stability independent of phosphatase activity of PpV, by competing with the catalytic subunit of PP2A for Wdb association, leading to Wdb ubiquitination and subsequent proteasomal degradation. Thus, regulated Wdb stability, maintained through competition between two closely related phosphatases, ensures graded Hh signaling. Interestingly, PpV expression is regulated by Hh signaling. Therefore, PpV functions as a Hh activity sensor that regulates Wdb-mediated PP2A activity through feedback mechanisms to maintain Hh signaling homeostasis.


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