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Related Concept Videos

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Covalently Linked Protein Regulators

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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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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The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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p57Kip2 Phosphorylation Modulates Its Localization, Stability, and Interactions.

Emanuela Stampone1, Debora Bencivenga1, Luisa Dassi1

  • 1Department of Precision Medicine, University of Campania "Luigi Vanvitelli", 80138 Naples, Italy.

International Journal of Molecular Sciences
|October 26, 2024
PubMed
Summary
This summary is machine-generated.

Human p57Kip2 protein is extensively phosphorylated, unlike its family members p21Cip1/WAF1 and p27Kip1. Its phosphorylation state affects binding to partners like CDKs, influencing cellular roles.

Keywords:
CIP/KipPTMcell cyclep57Kip2phosphorylationtwo-dimensional analysis

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • p57Kip2 is a member of the cyclin-dependent kinase (CDK) Inhibitor Protein (CIP/Kip) family.
  • p57Kip2 is an intrinsically unstructured protein (IUP) with limited data available, especially in humans.
  • Post-translational modifications, particularly phosphorylation, are crucial for IUPs like p57Kip2, affecting localization, stability, and interactions.

Purpose of the Study:

  • To investigate the phosphorylation pattern of human p57Kip2.
  • To compare the phosphorylation of p57Kip2 with p21Cip1/WAF1 and p27Kip1.
  • To understand how p57Kip2 phosphorylation influences its interactions with binding partners.

Main Methods:

  • Two-dimensional gel electrophoresis was used to analyze the phosphorylation pattern of p57Kip2.
  • Phosphoisoform distribution was examined in cytosolic and nuclear compartments of asynchronous and synchronized cells.
  • Interactions between p57Kip2 and its partners (CDKs, LIMK1, CRM1) were assessed in relation to phosphorylation state.

Main Results:

  • Human p57Kip2 is extensively phosphorylated compared to p21Cip1/WAF1 and p27Kip1.
  • Distinct phosphoisoform distributions were observed in the nucleus (unmodified form) and cytoplasm (acidic forms).
  • The phosphorylation state of p57Kip2 significantly impacts its binding affinity to partners like CDKs, LIMK1, and CRM1.

Conclusions:

  • p57Kip2 exhibits a unique and extensive phosphorylation profile within the CIP/Kip family.
  • Differential localization of p57Kip2 phosphoisoforms suggests compartment-specific regulatory roles.
  • Identifying specific phosphorylated residues is essential to fully elucidate the functions of p57Kip2 and its interactions.