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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
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The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
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Interactions Between Signaling Pathways

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Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
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Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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P21 activated kinases: structure, regulation, and functions.

Chetan K Rane1, Audrey Minden1

  • 1Susan Lehman Cullman Laboratory for Cancer Research; Department of Chemical Biology; Ernest Mario School of Pharmacy; Rutgers The State University of New Jersey; Piscataway, NJ USA.

Small Gtpases
|March 25, 2014
PubMed
Summary

p21 activated kinases (Paks) are crucial for cell growth and development. This review details Pak structures and their roles in cell biology and cancer.

Keywords:
neurobiologyoncogenesisp21-activated kinasespakprotein kinasessubstrates

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • p21 activated kinases (Paks) are effector proteins for Rho GTPases Cdc42 and Rac.
  • Paks comprise six members in two families: Paks 1-3 and Paks 4-6.
  • Paks are expressed in various tissues, with notable presence in the nervous system.

Purpose of the Study:

  • To review the basic structures of Paks.
  • To discuss the roles of Paks in cell growth and development.
  • To explore the involvement of Paks in cancer.

Main Methods:

  • Literature review of studies using cell culture.
  • Analysis of data from transgenic and knockout mouse models.
  • Synthesis of existing research on Pak protein functions.

Main Results:

  • Paks play significant roles in cytoskeletal organization.
  • Paks are implicated in diverse aspects of cell growth and development.
  • Pak dysregulation is linked to cancer progression.

Conclusions:

  • Paks are essential regulators of cellular processes.
  • Understanding Pak structure and function is key to cell biology and cancer research.
  • Further investigation into Paks may reveal therapeutic targets for cancer.