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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...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
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.
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...

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Updated: Jun 22, 2026

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
10:40

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

Type II transmembrane serine proteases.

Thomas H Bugge1, Toni M Antalis, Qingyu Wu

  • 1Proteases and Tissue Remodeling Section, NIDCR, National Institutes of Health, Bethesda, Maryland 20892, USA. thomas.bugge@nih.gov

The Journal of Biological Chemistry
|June 3, 2009
PubMed
Summary
This summary is machine-generated.

Type II transmembrane serine proteases (TTSPs) represent a newly identified protease family. Research has since expanded our understanding of TTSP functions and their role in human diseases.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genomics

Background:

  • The type II transmembrane serine proteases (TTSPs) family was first identified in 2001.
  • Since their discovery, the number of known TTSPs has more than doubled.
  • Significant advancements have been made in understanding TTSP physiological roles and disease associations.

Purpose of the Study:

  • To summarize the current knowledge on the rapidly advancing field of TTSPs.
  • To highlight progress in identifying molecular substrates and endogenous inhibitors of TTSPs.
  • To review the increasing understanding of TTSP involvement in human diseases.

Main Methods:

  • Analysis of genome and expressed sequence tag databases.
  • Literature review of published research on TTSPs.
  • Synthesis of current knowledge on TTSP functions, substrates, and inhibitors.

Main Results:

  • The TTSP family has expanded significantly since its initial discovery.
  • Understanding of individual TTSP physiological functions has greatly increased.
  • The contribution of TTSPs to human disease is becoming increasingly clear.

Conclusions:

  • TTSPs are a dynamic and expanding family of proteases with significant physiological roles.
  • Further research continues to uncover the complex involvement of TTSPs in human health and disease.
  • Continued investigation into TTSP substrates and inhibitors is crucial for understanding their biological impact.