STAMPing into Mitochondria

Six transmembrane protein of prostate 2 (STAMP2) is a protein that has been extensively studied due to its association with prostate cancer. Currently, STAMP2 is well known for its critical role in metabolism and modulating inflammatory signals. Even so, the molecular mechanism of STAMP2 activity an...

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Detalles Bibliográficos
Autores principales: Yoo, Seong Keun, Cheong, JaeHun, Kim, Hye Young
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Ivyspring International Publisher 2014
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3957087/
https://www.ncbi.nlm.nih.gov/pubmed/24643198
http://dx.doi.org/10.7150/ijbs.8456
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author Yoo, Seong Keun
Cheong, JaeHun
Kim, Hye Young
author_facet Yoo, Seong Keun
Cheong, JaeHun
Kim, Hye Young
author_sort Yoo, Seong Keun
collection PubMed
description Six transmembrane protein of prostate 2 (STAMP2) is a protein that has been extensively studied due to its association with prostate cancer. Currently, STAMP2 is well known for its critical role in metabolism and modulating inflammatory signals. Even so, the molecular mechanism of STAMP2 activity and its downstream effectors are still largely unknown. Here, we review the current knowledge of STAMP2, and suggest possible explanations for some of its less well-understood features. A few studies suggest that STAMP2 may interact with mitochondria. Considering STAMP2 functions as a potential component of mitochondrial biology may yield valuable insight into this protein.
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spelling pubmed-39570872014-03-18 STAMPing into Mitochondria Yoo, Seong Keun Cheong, JaeHun Kim, Hye Young Int J Biol Sci Review Six transmembrane protein of prostate 2 (STAMP2) is a protein that has been extensively studied due to its association with prostate cancer. Currently, STAMP2 is well known for its critical role in metabolism and modulating inflammatory signals. Even so, the molecular mechanism of STAMP2 activity and its downstream effectors are still largely unknown. Here, we review the current knowledge of STAMP2, and suggest possible explanations for some of its less well-understood features. A few studies suggest that STAMP2 may interact with mitochondria. Considering STAMP2 functions as a potential component of mitochondrial biology may yield valuable insight into this protein. Ivyspring International Publisher 2014-03-08 /pmc/articles/PMC3957087/ /pubmed/24643198 http://dx.doi.org/10.7150/ijbs.8456 Text en © Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited.
spellingShingle Review
Yoo, Seong Keun
Cheong, JaeHun
Kim, Hye Young
STAMPing into Mitochondria
title STAMPing into Mitochondria
title_full STAMPing into Mitochondria
title_fullStr STAMPing into Mitochondria
title_full_unstemmed STAMPing into Mitochondria
title_short STAMPing into Mitochondria
title_sort stamping into mitochondria
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3957087/
https://www.ncbi.nlm.nih.gov/pubmed/24643198
http://dx.doi.org/10.7150/ijbs.8456
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