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Related Concept Videos

Catenins01:23

Catenins

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.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Structure of Cadherins01:25

Structure of Cadherins

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 diversity of cadherins...

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Related Experiment Video

Updated: May 21, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

The N-terminus modulates human Caf1 activity, structural stability and aggregation.

Li-Kui Feng1, Yong-Bin Yan

  • 1State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Life Sciences, Tsinghua University, Beijing 100084, China.

International Journal of Biological Macromolecules
|June 12, 2012
PubMed
Summary
This summary is machine-generated.

The N-terminus of human Caf1 (hCaf1), a deadenylase, is crucial for its activity and stability. Removing it reduces hCaf1 function and thermal stability, impacting its role in the CCR4-Not complex.

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Last Updated: May 21, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Mass Spectrometry Analysis to Identify Ubiquitylation of EYFP-tagged CENP-A (EYFP-CENP-A)
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Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Caf1 is a key deadenylase subunit of the CCR4-Not complex, involved in gene regulation.
  • The CCR4-Not complex plays a vital role in cellular processes, including mRNA deadenylation.

Purpose of the Study:

  • To investigate the role of the N-terminus of human Caf1 (hCaf1) in its enzymatic activity, structural integrity, and stability.
  • To understand how the N-terminus influences hCaf1's thermal aggregation properties.

Main Methods:

  • Enzymatic activity assays were performed to quantify hCaf1 activity.
  • Thermal stability was assessed to determine the impact of N-terminus removal.
  • Homology modeling was utilized to predict the structural contribution of the N-terminus.

Main Results:

  • Removal of the hCaf1 N-terminus caused a 30% reduction in deadenylase activity.
  • N-terminus removal decreased thermal stability and reduced thermal aggregation.
  • Homology modeling suggested the N-terminus can form an alpha-helix interacting with the main domain.

Conclusions:

  • The N-terminus of hCaf1 is essential for modulating its enzymatic activity and thermal stability.
  • The N-terminus influences hCaf1's propensity for thermal aggregation.
  • These findings provide insights into the structural and functional regulation of Caf1 within the CCR4-Not complex.