Escorting Ras
Ras proteins are best known to function on the plasma membrane to mediate growth factor signaling. Controlling the length of time that Ras proteins stay on the plasma membrane is an effective way to properly modulate the intensity and duration of growth factor signaling. It has been shown previously...
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| Format: | Online |
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Landes Bioscience
2012
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3520888/ |
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pubmed-35208882012-12-17 Escorting Ras Zheng, Ze-Yi Xu, Lizhong Bar-Sagi, Dafna Chang, Eric C. Commentary Ras proteins are best known to function on the plasma membrane to mediate growth factor signaling. Controlling the length of time that Ras proteins stay on the plasma membrane is an effective way to properly modulate the intensity and duration of growth factor signaling. It has been shown previously that H- and N-Ras proteins in the GTP-bound state can be ubiquitylated via a K-63 linkage, which leads to endosome internalization and results in a negative-feedback loop for efficient signal attenuation. In a more recent study, two new Ras effectors have been isolated, CHMP6 and VPS4A, which are components of the ESCRT-III complex, best known for mediating protein sorting in the endosomes. Surprisingly, these molecules are required for efficient Ras-induced transformation. They apparently do so by controlling recycling of components of the Ras pathway back to the plasma membrane, thus creating a positive-feedback loop to enhance growth factor signaling. These results suggest the fates of endosomal Ras proteins are complex and dynamic — they can be either stored and/or destroyed or recycled. Further work is needed to decipher how the fate of these endosomal Ras proteins is determined. Landes Bioscience 2012-10-01 /pmc/articles/PMC3520888/ /pubmed/22735486 http://dx.doi.org/10.4161/sgtp.20460 Text en Copyright © 2012 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Zheng, Ze-Yi Xu, Lizhong Bar-Sagi, Dafna Chang, Eric C. |
| spellingShingle |
Zheng, Ze-Yi Xu, Lizhong Bar-Sagi, Dafna Chang, Eric C. Escorting Ras |
| author_facet |
Zheng, Ze-Yi Xu, Lizhong Bar-Sagi, Dafna Chang, Eric C. |
| author_sort |
Zheng, Ze-Yi |
| title |
Escorting Ras |
| title_short |
Escorting Ras |
| title_full |
Escorting Ras |
| title_fullStr |
Escorting Ras |
| title_full_unstemmed |
Escorting Ras |
| title_sort |
escorting ras |
| description |
Ras proteins are best known to function on the plasma membrane to mediate growth factor signaling. Controlling the length of time that Ras proteins stay on the plasma membrane is an effective way to properly modulate the intensity and duration of growth factor signaling. It has been shown previously that H- and N-Ras proteins in the GTP-bound state can be ubiquitylated via a K-63 linkage, which leads to endosome internalization and results in a negative-feedback loop for efficient signal attenuation. In a more recent study, two new Ras effectors have been isolated, CHMP6 and VPS4A, which are components of the ESCRT-III complex, best known for mediating protein sorting in the endosomes. Surprisingly, these molecules are required for efficient Ras-induced transformation. They apparently do so by controlling recycling of components of the Ras pathway back to the plasma membrane, thus creating a positive-feedback loop to enhance growth factor signaling. These results suggest the fates of endosomal Ras proteins are complex and dynamic — they can be either stored and/or destroyed or recycled. Further work is needed to decipher how the fate of these endosomal Ras proteins is determined. |
| publisher |
Landes Bioscience |
| publishDate |
2012 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3520888/ |
| _version_ |
1611939966391156736 |