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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
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The Hedgehog gene (Hh) was first discovered due to its control of the growth of disorganized, hair-like bristles phenotype in Drosophila, much like hedgehog spines. Hh plays a crucial role in the development of organs and the maintenance of homeostasis in both invertebrates and vertebrates. However, while Drosophila has only one Hh protein, mammals have multiple functional Hedgehog proteins - Sonic (Shh), Desert (Dhh), and Indian Hedgehog (Ihh). All of these homologous proteins have adapted to...
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Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated...
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The cadherins are a superfamily of cell adhesion molecules comprising over 180 variants, with specific tissues expressing a particular combination of cadherin types. Cadherins generally exhibit homophilic binding; i.e., cadherins on one cell bind to cadherins of the same or closely related type on another cell. Thus, cells of the same type have a specific affinity to bind to each other and sort themselves into clusters to form tissues.
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Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
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Cdh1 controls the stability of TACC3.

Jen-Chong Jeng1, Ying-Mei Lin, Chiou-Hong Lin

  • 1Graduate Institute of Life Sciences, National Defense Medical Center and Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan, Republic of China.

Cell Cycle (Georgetown, Tex.)
|October 14, 2009
PubMed
Summary

The study reveals that Cdh1 regulates the protein level of Transforming acidic coiled-coil protein 3 (TACC3). Cdh1 controls TACC3 stability during mitotic exit, impacting cell division.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Transforming acidic coiled-coil protein 3 (TACC3) is crucial for mitotic spindle assembly and chromosome segregation.
  • The precise mechanisms controlling TACC3 protein levels during the cell cycle remain largely unknown.

Purpose of the Study:

  • To elucidate the molecular mechanisms regulating TACC3 protein stability.
  • To identify factors that control TACC3 levels during cell cycle progression.

Main Methods:

  • Yeast array screening to identify interacting partners.
  • In vitro and in vivo binding assays to confirm TACC3-Cdh1 complex formation.
  • Depletion and overexpression studies of Cdh1, alongside ubiquitination assays and domain mapping of TACC3.

Main Results:

  • Cdh1 was identified as a TACC3 interacting partner.
  • TACC3 forms complexes with Cdh1 both in vitro and in vivo.
  • Cdh1 depletion increases TACC3 protein levels during mitotic exit.
  • Cdh1 levels inversely correlate with TACC3 ubiquitination, indicating a role in degradation.
  • Multiple domains of TACC3 are involved in Cdh1-mediated degradation.

Conclusions:

  • Cdh1 acts as a key regulator of TACC3 protein stability.
  • Cdh1 promotes the degradation of TACC3 during mitotic exit.
  • This regulation is critical for proper cell cycle progression and chromosome segregation.