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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...

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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

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Stomatin-domain proteins.

Liudmilla Lapatsina1, Janko Brand, Kate Poole

  • 1Department of Neuroscience, Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Str. 10, 13092 Berlin-Buch, Germany.

European Journal of Cell Biology
|April 20, 2011
PubMed
Summary
This summary is machine-generated.

Stomatin-domain proteins are found across all life forms and may share a common cellular role. Research suggests these proteins oligomerize, localize to membrane domains, and modulate ion channel activity, though mechanisms remain unclear.

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Image-Based Methods to Study Membrane Trafficking Events in Stomatal Lineage Cells
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Image-Based Methods to Study Membrane Trafficking Events in Stomatal Lineage Cells

Published on: May 12, 2023

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Stomatin-domain proteins are conserved across all life classes.
  • Mammalian genomes contain five distinct stomatin family proteins with varied expression and localization.
  • The unifying cellular function of stomatin-domain proteins remains undefined.

Purpose of the Study:

  • To review and synthesize current literature on stomatin-domain proteins.
  • To identify common themes in stomatin protein behavior and function.
  • To highlight knowledge gaps regarding their cellular roles.

Main Methods:

  • Literature survey and analysis of existing research on stomatin-domain proteins.
  • Identification of recurring characteristics such as oligomerization and membrane localization.
  • Review of studies investigating the interaction of stomatin proteins with ion channels.

Main Results:

  • Stomatin family members exhibit oligomeric structures.
  • These proteins predominantly localize to specific membrane domains.
  • Evidence indicates stomatin proteins modulate ion channel activity.

Conclusions:

  • Oligomerization and membrane localization are key features of stomatin proteins.
  • The precise mechanisms by which stomatin proteins influence ion channels are not yet understood.
  • Further research into the structure and function of stomatin-like proteins is needed to elucidate their cellular roles.