MST4
MST4 is a protein that in humans is encoded by the MST4 gene. This protein belongs to the serine/threonine protein kinase family and plays a significant role in various cellular processes, including cell proliferation, differentiation, and apoptosis. The MST4 gene and its protein product are crucial for the proper functioning of several signaling pathways that regulate cell growth and survival.
Function[edit | edit source]
MST4 kinase is involved in the regulation of the cytoskeleton, an essential component of cell structure and movement. It has been shown to phosphorylate and activate members of the AGC kinase family, which includes proteins such as AKT and PKC, implicating MST4 in the control of cell shape, motility, and possibly the cell cycle. Furthermore, MST4 can interact with and phosphorylate other substrates such as MOBKL1A/B, which are involved in the Hippo signaling pathway, a critical regulator of organ size and tumor suppression.
Clinical Significance[edit | edit source]
Alterations in the expression or activity of MST4 have been implicated in various human diseases, including cancer. Overexpression of MST4 has been observed in certain types of cancer, suggesting a potential role in tumorigenesis. Conversely, MST4's involvement in the Hippo pathway highlights its possible function in tumor suppression, indicating that the context-dependent regulation of MST4 activity could influence cancer development and progression.
Additionally, due to its role in cell motility and cytoskeletal regulation, MST4 may also be involved in wound healing and the response to tissue injury. Its precise functions in these processes, however, remain to be fully elucidated.
Gene[edit | edit source]
The MST4 gene is located on human chromosome 2, and like other kinases, it encodes a protein with a kinase domain necessary for its enzymatic activity. The regulation of MST4 expression and activity is complex and involves various post-translational modifications and interactions with other cellular proteins.
Interaction[edit | edit source]
MST4 has been shown to interact with several proteins, including STRN (striatin), STRN3 (striatin 3), and CTTN (cortactin), which are involved in the regulation of cell morphology and motility. These interactions suggest a role for MST4 in the dynamic reorganization of the actin cytoskeleton, which is crucial for cell movement and adhesion.
Research Directions[edit | edit source]
Ongoing research aims to further elucidate the biological functions of MST4, its regulatory mechanisms, and its role in disease. Understanding the precise molecular pathways involving MST4 could lead to the development of novel therapeutic strategies for cancer and other diseases associated with aberrant cell growth and migration.
Search WikiMD
Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro / Zepbound) available.
Advertise on WikiMD
WikiMD's Wellness Encyclopedia |
Let Food Be Thy Medicine Medicine Thy Food - Hippocrates |
Translate this page: - East Asian
中文,
日本,
한국어,
South Asian
हिन्दी,
தமிழ்,
తెలుగు,
Urdu,
ಕನ್ನಡ,
Southeast Asian
Indonesian,
Vietnamese,
Thai,
မြန်မာဘာသာ,
বাংলা
European
español,
Deutsch,
français,
Greek,
português do Brasil,
polski,
română,
русский,
Nederlands,
norsk,
svenska,
suomi,
Italian
Middle Eastern & African
عربى,
Turkish,
Persian,
Hebrew,
Afrikaans,
isiZulu,
Kiswahili,
Other
Bulgarian,
Hungarian,
Czech,
Swedish,
മലയാളം,
मराठी,
ਪੰਜਾਬੀ,
ગુજરાતી,
Portuguese,
Ukrainian
Medical Disclaimer: WikiMD is not a substitute for professional medical advice. The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes. Please consult your health care provider before making any healthcare decisions or for guidance about a specific medical condition. WikiMD expressly disclaims responsibility, and shall have no liability, for any damages, loss, injury, or liability whatsoever suffered as a result of your reliance on the information contained in this site. By visiting this site you agree to the foregoing terms and conditions, which may from time to time be changed or supplemented by WikiMD. If you do not agree to the foregoing terms and conditions, you should not enter or use this site. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.
Contributors: Prab R. Tumpati, MD