Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
Mitochondrial Membranes01:45

Mitochondrial Membranes

A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
Mitochondrial Membranes01:45

Mitochondrial Membranes

A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
What are Membranes?01:24

What are Membranes?

A cell's plasma membrane demarcates the cell's borders and determines the nature of its interaction with the environment. Cells exclude certain substances, take in others, and excrete some others in controlled quantities. The plasma membrane must be flexible to allow certain cells, such as red and white blood cells, to change their shape while passing through narrow capillaries. These are the more obvious plasma membrane functions. In addition, the plasma membrane's surface carries markers that...
What are Membranes?01:54

What are Membranes?

A key characteristic of life is the ability to separate the external environment from the internal space. To do this, cells have evolved semi-permeable membranes that regulate the passage of biological molecules. Additionally, the cell membrane defines a cell’s shape and interactions with the external environment. Eukaryotic cell membranes also serve to compartmentalize the internal space into organelles, including the endomembrane structures of the nucleus, endoplasmic reticulum and Golgi...
What are Membranes?01:24

What are Membranes?

A cell's plasma membrane demarcates the cell's borders and determines the nature of its interaction with the environment. Cells exclude certain substances, take in others, and excrete some others in controlled quantities. The plasma membrane must be flexible to allow certain cells, such as red and white blood cells, to change their shape while passing through narrow capillaries. These are the more obvious plasma membrane functions. In addition, the plasma membrane's surface carries markers that...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Low-dose carboplatin modifies the tumor microenvironment to augment CAR T cell efficacy in human prostate cancer models.

Nature communications·2023
Same author

Early-phenotype CAR-T cells for the treatment of pediatric cancers.

Annals of oncology : official journal of the European Society for Medical Oncology·2021
Same author

Perforin inhibition protects from lethal endothelial damage during fulminant viral hepatitis.

Nature communications·2018
Same author

Chimeric antigen receptor T cells form nonclassical and potent immune synapses driving rapid cytotoxicity.

Proceedings of the National Academy of Sciences of the United States of America·2018
Same author

A genome scale RNAi screen identifies GLI1 as a novel gene regulating vorinostat sensitivity.

Cell death and differentiation·2016
Same author

In memoriam: Prof Christopher J Froelich (1951-2015).

Cell death and differentiation·2015

Related Experiment Video

Updated: Jun 8, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
08:53

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

The structure and function of mammalian membrane-attack complex/perforin-like proteins.

S C Kondos1, T Hatfaludi, I Voskoboinik

  • 1Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia.

Tissue Antigens
|September 24, 2010
PubMed
Summary

The membrane-attack complex (MAC) and perforin (PF) use MACPF domains to form pores, targeting pathogens and infected cells. This review explores the diverse roles and structures of mammalian MACPF proteins in immunity and development.

More Related Videos

High-throughput Measurement of Plasma Membrane Resealing Efficiency in Mammalian Cells
10:07

High-throughput Measurement of Plasma Membrane Resealing Efficiency in Mammalian Cells

Published on: January 7, 2019

Live Imaging Assay for Assessing the Roles of Ca2+ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds
18:25

Live Imaging Assay for Assessing the Roles of Ca2+ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds

Published on: August 25, 2013

Related Experiment Videos

Last Updated: Jun 8, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
08:53

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

High-throughput Measurement of Plasma Membrane Resealing Efficiency in Mammalian Cells
10:07

High-throughput Measurement of Plasma Membrane Resealing Efficiency in Mammalian Cells

Published on: January 7, 2019

Live Imaging Assay for Assessing the Roles of Ca2+ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds
18:25

Live Imaging Assay for Assessing the Roles of Ca2+ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds

Published on: August 25, 2013

Area of Science:

  • Immunology
  • Structural Biology
  • Developmental Biology

Background:

  • The membrane-attack complex (MAC) and perforin (PF) are key immune effectors utilizing the MACPF domain to form transmembrane pores.
  • Both MAC and PF target pathogens and host cells, respectively, playing crucial roles in innate and adaptive immunity.
  • The MACPF domain shares homology with bacterial cytolysins, offering insights into pore formation mechanisms.

Purpose of the Study:

  • To review the structural and functional diversity of mammalian MACPF proteins.
  • To elucidate the varied roles of MACPF proteins beyond pore formation, particularly in developmental processes.
  • To bridge the understanding between the pore-forming capabilities and non-pore-forming functions of MACPF family members.

Main Methods:

  • Literature review of structural and functional studies on MACPF proteins.
  • Comparative analysis of MACPF domain homology with other pore-forming proteins.
  • Synthesis of current knowledge on MACPF protein functions in immunity and development.

Main Results:

  • MACPF proteins exhibit significant structural and functional diversity, with some forming pores and others not.
  • Beyond immunity, MACPF proteins are implicated in diverse biological processes including venom activity, pathogen invasion, and embryonic development.
  • Structural homology to cytolysins provides a mechanistic basis for the pore-forming function of certain MACPF proteins.

Conclusions:

  • Mammalian MACPF proteins are a versatile family with critical roles in both immune defense and complex biological processes.
  • Understanding the non-pore-forming functions of MACPF proteins is essential for comprehending their broader biological significance.
  • Further research into MACPF protein structure-function relationships will illuminate their roles in health and disease.