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Related Concept Videos

Phosphorylation01:02

Phosphorylation

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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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Protein Kinases and Phosphatases02:54

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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.
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PI3K/mTOR/AKT Signaling Pathway01:22

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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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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
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Phosphoinositides and PIPs01:42

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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
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Asp/ASPM phospho-regulation throughout the cell cycle.

Maria C Burns1, Lori Borgal1

  • 1Department of Biology, Mount St. Vincent University, Halifax, NS B3M 2J6, Canada.

Genome
|October 29, 2024
PubMed
Summary

Asp/ASPM proteins regulate cell division and spindle formation. This review suggests cyclin-dependent kinases (CDKs) regulate Asp/ASPM, impacting cell cycle roles and potentially causing microcephaly and cancer.

Keywords:
ASPMAspCDK1cell cyclespindle

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Asp/ASPM proteins are crucial for cell proliferation and spindle formation in mammals and Drosophila.
  • Emerging evidence indicates Asp/ASPM proteins also have interphase roles, but their regulation across cell cycle phases remains unclear.

Purpose of the Study:

  • To explore the regulation of Asp/ASPM proteins across different cell cycle phases.
  • To investigate the potential role of cyclin-dependent kinases (CDK) in regulating Asp/ASPM functions.
  • To hypothesize new regulatory mechanisms for Asp/ASPM in interphase and mitosis, and their dysregulation in disease.

Main Methods:

  • Cross-species comparative analysis of Asp/ASPM protein sequences.
  • Integration with existing cyclin-CDK literature.
  • In silico structural predictions of human, mouse, and Drosophila Asp/ASPM proteins.
  • Analysis of microcephaly patient truncation structures.

Main Results:

  • Identified conserved N-terminal S/T-P phosphorylation "supershift" domains and putative cyclin-binding sites in Asp/ASPM proteins.
  • Structural predictions suggest multisite phosphorylation can alter CH-domains and HEAT-motifs, influencing microtubule binding and protein aggregation.
  • The arrangement of these motifs is critical, as highlighted by microcephaly patient structural data.

Conclusions:

  • Asp/ASPM proteins are strong candidates for regulation by cyclin-CDKs, enabling distinct roles in interphase and mitosis.
  • Multisite phosphorylation of the N-terminal domain may control Asp/ASPM's interaction with cellular components.
  • Understanding Asp/ASPM regulation provides insights into microcephaly, cancer, and potential therapeutic strategies.