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

Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

4.1K
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...
4.1K
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

7.3K
Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
7.3K
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

19.0K
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...
19.0K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

13.8K
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,...
13.8K
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

3.9K
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
3.9K
Structure of Porins01:21

Structure of Porins

4.2K
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...
4.2K

You might also read

Related Articles

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

Sort by
Same author

Calcium dependent activation of the TMEM16F scramblase and ion channel.

Nature structural & molecular biology·2026
Same author

Dominant Action of <i>CLCN4</i> Neurodevelopmental Disease Variants in Heteromeric Endosomal ClC-3/ClC-4 Transporters.

Cells·2025
Same author

FGF13 is not secreted from neurons.

bioRxiv : the preprint server for biology·2025
Same author

FGF13 is not secreted from mouse neurons.

JCI insight·2025
Same author

FGF13 Regulates VGSC-Independent Cardiomyocyte Impulse Propagation via Cx43 Trafficking.

Circulation research·2025
Same author

The NaV1.5 auxiliary subunit FGF13 modulates channels by regulating membrane cholesterol independent of channel binding.

The Journal of clinical investigation·2025

Related Experiment Video

Updated: Apr 20, 2026

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

3.0K

TMEM16 proteins: unknown structure and confusing functions.

Alessandra Picollo1, Mattia Malvezzi2, Alessio Accardi3

  • 1Department of Anesthesiology, Weill Cornell Medical College, 1300 York Avenue, New York, NY 10065, USA.

Journal of Molecular Biology
|December 3, 2014
PubMed
Summary
This summary is machine-generated.

The TMEM16 (anoctamin) family of proteins functions in ion transport and lipid scrambling. This diverse family may have evolved into subclasses of channels, scramblases, or dual-function proteins, impacting human health.

Keywords:
Ca(2+)-activated Cl(−) channelsCa(2+)-dependent phospholipid scramblinganoctaminmembrane proteinsreconstitution

More Related Videos

Author Spotlight: Unveiling Transmembrane Protein Family-Related Markers in Gastric Cancer and Implications for Targeted Therapies
07:47

Author Spotlight: Unveiling Transmembrane Protein Family-Related Markers in Gastric Cancer and Implications for Targeted Therapies

Published on: September 15, 2023

2.4K
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.5K

Related Experiment Videos

Last Updated: Apr 20, 2026

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

3.0K
Author Spotlight: Unveiling Transmembrane Protein Family-Related Markers in Gastric Cancer and Implications for Targeted Therapies
07:47

Author Spotlight: Unveiling Transmembrane Protein Family-Related Markers in Gastric Cancer and Implications for Targeted Therapies

Published on: September 15, 2023

2.4K
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.5K

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • The TMEM16 family, also known as anoctamins, comprises membrane proteins crucial for physiological processes.
  • TMEM16A (ANO1) and TMEM16B (ANO2) are well-characterized Ca(2+)-activated Cl(-) channels involved in various functions.
  • The roles of other TMEM16 family members are less understood, with reported functions including ion channel activity, phospholipid scrambling, or both.

Purpose of the Study:

  • To review the known and proposed functions of the TMEM16 (anoctamin) protein family.
  • To explore the potential functional divergence within the TMEM16 family, possibly into channels, scramblases, or dual-function proteins.
  • To highlight the need for further investigation into the structural basis, functional implications, and links to human diseases of TMEM16 family members.

Main Methods:

  • Literature review and synthesis of existing research on TMEM16 proteins.
  • Analysis of functional data from studies on various TMEM16 family members.
  • Hypothesis generation regarding the evolutionary divergence and functional classification of TMEM16 proteins.

Main Results:

  • TMEM16A and TMEM16B are established Ca(2+)-activated Cl(-) channels with roles in diverse physiological processes.
  • Evidence suggests TMEM16F may act as a phospholipid scramblase, as seen in Scott syndrome, but also exhibits ion channel activity.
  • An ancestral TMEM16 homolog with both channel and scramblase activity supports the hypothesis of functional diversification within the family.

Conclusions:

  • The TMEM16 family likely encompasses distinct subclasses: ion channels, phospholipid scramblases, and proteins with dual functions.
  • Understanding the functional diversity and structural basis of TMEM16 proteins is critical.
  • Further research is needed to elucidate the roles of TMEM16 proteins in human physiology and pathology.