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Related Concept Videos

Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

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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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Covalently Linked Protein Regulators02:04

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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.
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Enlargement of the Plasma Membrane01:22

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Cell division and enlargement are processes that require precise control. The control ensures that cell division cannot proceed unless the cell has grown to a specific size. A spherical, dividing cell requires an approximately 1.6X increase in its surface area to double its volume. The secretory pathway also has a significant role in cell membrane enlargement. Secretory vesicles that bud off from the Golgi apparatus and later fuse with the plasma membrane during exocytosis are a major source of...
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Plasma Membrane in Bacteria and Archaea01:27

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The plasma membrane is an essential cellular structure responsible for maintaining cellular integrity and regulating the selective transport of molecules. While bacteria and archaea share the fundamental function of plasma membranes, their structural and molecular differences reflect adaptations to distinct ecological and physiological challenges.Bacterial Plasma MembranesBacterial plasma membranes are predominantly composed of phospholipids with fatty acid chains ester-linked to a glycerol...
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Fusion of Secretory Vesicles with the Plasma Membrane01:26

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Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
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Related Experiment Video

Updated: Feb 8, 2026

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins
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Lateral plasma membrane compartmentalization links protein function and turnover.

Jon V Busto1,2, Annegret Elting1, Daniel Haase1

  • 1Institute of Cell Dynamics and Imaging, Cells-In-Motion Cluster of Excellence (EXC1003 - CiM), University of Münster, Münster, Germany.

The EMBO Journal
|July 7, 2018
PubMed
Summary
This summary is machine-generated.

Biological membranes form distinct domains that regulate protein function and turnover. In yeast, the methionine permease Mup1 clusters in specific domains, which protects it from degradation until it relocates and initiates its own turnover.

Keywords:
amino acid permeaseendocytosislateral membrane segregationpatchwork membraneplasma membrane

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Area of Science:

  • Cell biology
  • Biochemistry
  • Membrane biology

Background:

  • Biological membranes exhibit complex lipid and protein organization into nano- and microdomains.
  • The functional significance of plasma membrane (PM) compartmentalization in yeast is not fully understood.
  • Understanding how PM organization impacts protein regulation is crucial.

Purpose of the Study:

  • To investigate the relationship between PM compartmentalization, protein function, and endocytic turnover in yeast.
  • To elucidate the mechanisms regulating the localization and stability of the methionine permease Mup1.
  • To determine the role of sphingolipids, Nce102, and TORC2 signaling in Mup1 compartmentalization.

Main Methods:

  • Utilized the methionine permease Mup1 as a model system in yeast.
  • Investigated Mup1's segregation into PM clusters and its relocation dynamics.
  • Analyzed the role of sphingolipids, Nce102, and TORC2 in Mup1 clustering.
  • Examined the recruitment of endocytic machinery to Mup1.

Main Results:

  • Mup1 segregates into distinct PM clusters, requiring sphingolipids, Nce102, and TORC2 signaling.
  • Substrate transport induces a conformational change in Mup1, leading to relocation into a disperse network.
  • Clustered Mup1 is protected from turnover, while relocated Mup1 initiates its own endocytosis.
  • Lateral compartmentalization directly links PM protein function and turnover.

Conclusions:

  • Plasma membrane compartmentalization plays a critical role in regulating protein turnover.
  • Mup1's localization and conformational state dictate its stability and endocytic fate.
  • This study reveals a novel regulatory mechanism linking membrane organization to protein lifecycle.