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Related Concept Videos

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
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The Supercomplexes in the Crista Membrane01:41

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The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
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Insertion of Multi-pass Transmembrane Proteins in the RER01:29

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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.
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Tail-anchoring of Proteins in the ER Membrane01:45

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

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ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
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Biochemical Structure and Function of TRAPP Complexes in the Cardiac System.

Peter Papaioannou1,2, Michael J Wallace1,3, Nipun Malhotra1,2

  • 1Frick Center for Heart Failure and Arrhythmia Research, Dorothy M. Davis Heart and Lung Research Institute, The Ohio State University Wexner Medical Center, Columbus, Ohio, USA.

JACC. Basic to Translational Science
|January 11, 2024
PubMed
Summary

Trafficking protein particle (TRAPP) complexes are vital for cellular transport. This study explores TRAPP

Keywords:
Kv1.5Kv4.2Rab1Rab11TRAPP

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cardiovascular Science

Background:

  • Trafficking protein particle (TRAPP) complexes mediate protein transport within the Golgi and endoplasmic reticulum.
  • TRAPP dysfunction is linked to nervous and cardiovascular system disorders, yet research predominantly focuses on neurological roles.
  • The specific cardiovascular implications of TRAPP dysfunction remain underexplored.

Purpose of the Study:

  • To elucidate the role of TRAPP in cardiovascular function.
  • To investigate TRAPP's potential impact on cardiovascular diseases.
  • To highlight TRAPP's function as a guanine-nucleotide exchange factor for Rab1 and Rab11 in the cardiovascular context.

Main Methods:

  • Literature review of TRAPP pathways and functions.
  • Analysis of existing research on TRAPP and cardiovascular phenotypes.
  • Hypothesizing the impact of TRAPP dysfunction on cardiovascular systems.

Main Results:

  • TRAPP complexes are crucial for intracellular trafficking.
  • TRAPP acts as a guanine-nucleotide exchange factor for Rab1 and Rab11.
  • Alterations in TRAPP complexes and subunits are associated with various cardiovascular phenotypes.

Conclusions:

  • TRAPP plays a significant, yet underappreciated, role in cardiovascular health.
  • Further research into TRAPP's cardiovascular functions is warranted.
  • Understanding TRAPP's role may offer new therapeutic targets for cardiovascular diseases.