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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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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...
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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.
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The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell...
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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.
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Neutron Spin Echo Spectroscopy as a Unique Probe for Lipid Membrane Dynamics and Membrane-Protein Interactions
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SMP domain proteins in membrane lipid dynamics.

Darshini Jeyasimman1, Yasunori Saheki2

  • 1Lee Kong Chian School of Medicine, Nanyang Technological University, 308232, Singapore.

Biochimica Et Biophysica Acta. Molecular and Cell Biology of Lipids
|April 20, 2019
PubMed
Summary

Synaptotagmin-like mitochondrial-lipid-binding (SMP) domain proteins are key lipid transporters at membrane contact sites. This review covers their functions, lipid transport mechanisms, and physiological roles in eukaryotes.

Keywords:
ERLipid transportMembrane contact sitesSMPTULIP

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Synaptotagmin-like mitochondrial-lipid-binding (SMP) domain proteins are conserved eukaryotic proteins.
  • They localize to membrane contact sites, such as ER-plasma membrane junctions.
  • SMP proteins mediate membrane tethering via interactions with lipids and other proteins.

Purpose of the Study:

  • To review the functions of SMP domain proteins.
  • To summarize their roles in lipid transport across cellular compartments.
  • To discuss their physiological importance and related pathways.

Main Methods:

  • Literature review of structural and biochemical studies.
  • Analysis of existing research on SMP domain protein functions.
  • Synthesis of data on lipid transport and physiological roles.

Main Results:

  • SMP domain proteins possess a hydrophobic cavity for lipid binding and transport.
  • They are crucial for various lipid species transport between organelles.
  • Evidence highlights their critical roles in cell physiology at membrane contact sites.

Conclusions:

  • SMP domain proteins are essential lipid transporters at membrane contact sites.
  • Their functions are vital for cellular homeostasis and physiological processes.
  • Understanding SMP proteins offers insights into parallel pathways at membrane contact sites.