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

Golgi Matrix Proteins01:12

Golgi Matrix Proteins

2.0K
Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
2.0K
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

6.7K
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...
6.7K
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

4.6K
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
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
4.6K
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

8.0K
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...
8.0K
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

7.3K
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.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
7.3K
Transport Across the Golgi01:26

Transport Across the Golgi

4.2K
While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
4.2K

You might also read

Related Articles

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

Sort by
Same author

Inositol-requiring enzyme 1 alpha is essential for dentinogenesis.

Frontiers in physiology·2025
Same author

d-Band Optimized Hydrogen Adsorption and Dynamic Reconstruction-Accelerated Oxygen Evolution on RuS<sub>2</sub>/(FeNi)S<sub>1.03</sub> Heterointerfaces for Water/Seawater Splitting.

Small (Weinheim an der Bergstrasse, Germany)·2025
Same author

Constitutive expression of spliced X-box binding protein 1 inhibits dentin formation in mice.

Frontiers in physiology·2024
Same author

Intracranial calcification in Fam20c-deficient mice recapitulates human Raine syndrome.

Neuroscience letters·2023
Same author

Long-acting PFI-2 small molecule release and multilayer scaffold design achieve extensive new formation of complex periodontal tissues with unprecedented fidelity.

Biomaterials·2022
Same author

Correction to "Construction of a Cu-Sn Heterojunction Interface Derived from a Schottky Junction in Cu@Sn/rGO Composites as a Highly Efficient Dielectric Microwave Absorber".

ACS applied materials & interfaces·2022

Related Experiment Video

Updated: Jun 30, 2025

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein
07:20

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein

Published on: June 16, 2023

2.1K

FAM20A is a golgi-localized Type II transmembrane protein.

Mohammad Faizan Siddiqui1, Jiahe Li1, Suzhen Wang1

  • 1Department of Biomedical Sciences, Texas A&M University School of Dentistry, 3302 Gaston Ave, Dallas, TX, 75246, USA.

Scientific Reports
|March 19, 2024
PubMed
Summary
This summary is machine-generated.

Family with sequence similarity 20, member A (FAM20A) is a transmembrane protein in the secretory pathway. This study confirms FAM20A localizes to cellular membranes, crucial for its role in enamel formation.

More Related Videos

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
13:08

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

Published on: August 10, 2017

10.8K
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

2.5K

Related Experiment Videos

Last Updated: Jun 30, 2025

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein
07:20

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein

Published on: June 16, 2023

2.1K
Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
13:08

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

Published on: August 10, 2017

10.8K
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

2.5K

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Family with sequence similarity 20, member A (FAM20A) is a pseudo-kinase.
  • FAM20A plays a critical role in human enamel formation.
  • Its precise localization within the secretory pathway is not fully understood.

Purpose of the Study:

  • To investigate the subcellular localization of FAM20A.
  • To determine if FAM20A is a membrane-associated protein.
  • To elucidate the topology of FAM20A within secretory compartments.

Main Methods:

  • HEK293 cells were transfected with a FAM20A-expressing construct.
  • Cellular fractionation was performed to separate membrane and soluble fractions.
  • Immunofluorescence microscopy was used to assess co-localization with organelle markers (GM130).
  • Membrane topology analysis was conducted.

Main Results:

  • Full-length FAM20A was successfully purified from transfected HEK293 cells.
  • FAM20A was exclusively detected in the membrane fraction, not the soluble fraction.
  • FAM20A was not secreted from the expressing cells.
  • FAM20A co-localized with the cis-Golgi marker GM130.
  • Topology analysis revealed a C-terminus oriented towards the organelle lumen.

Conclusions:

  • FAM20A is a membrane-associated protein within the secretory pathway.
  • The findings support FAM20A being a Type II transmembrane protein.
  • This localization is consistent with its essential function in enamel formation.