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Related Concept Videos

Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...
Proteins: From Genes to Degradation02:11

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Transcription is the synthesis of RNA molecules by RNA...
The Proteasome02:18

The Proteasome

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The Proteasome01:13

The Proteasome

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Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.

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Updated: Jun 27, 2026

Purification of the Dendritic Filopodia-rich Fraction
11:51

Purification of the Dendritic Filopodia-rich Fraction

Published on: May 2, 2019

Presenilin: RIP and beyond.

Matthew R Hass1, Chihiro Sato, Raphael Kopan

  • 1Department of Developmental Biology, Washington University School of Medicine, Saint Louis, MO, United States.

Seminars in Cell & Developmental Biology
|December 17, 2008
PubMed
Summary
This summary is machine-generated.

Presenilins (PSENs) have functions beyond proteolysis, influencing cell signaling, beta-catenin, protein trafficking, calcium, and apoptosis. This review explores these diverse roles of PSEN proteins.

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Last Updated: Jun 27, 2026

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Published on: June 13, 2020

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Presenilins (PSENs) are multi-transmembrane domain proteins.
  • Their established role involves regulated intramembrane proteolysis via gamma-secretase.
  • Emerging evidence suggests broader cellular functions.

Purpose of the Study:

  • To review PSEN functions beyond regulated intramembrane proteolysis.
  • To discuss PSEN's role in modulating cellular signaling pathways.
  • To critically examine proposed roles in beta-catenin regulation, protein trafficking, calcium homeostasis, and apoptosis.

Main Methods:

  • Literature review of in vivo evidence.
  • Analysis of studies on gamma-secretase activity.
  • Critical evaluation of proposed PSEN functions.

Main Results:

  • PSENs modulate cellular signaling by cleaving transmembrane proteins via gamma-secretase.
  • Evidence supports PSEN involvement in beta-catenin regulation.
  • Proposed roles in protein trafficking, calcium regulation, and apoptosis are examined.

Conclusions:

  • PSENs possess diverse functions extending beyond their known proteolytic activity.
  • Understanding these roles is crucial for comprehending cellular regulation.
  • Further research is needed to fully elucidate PSEN's multifaceted contributions.