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Flippase
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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.
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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...
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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Functional swapping between transmembrane proteins TMEM16A and TMEM16F.

Takayuki Suzuki1, Jun Suzuki, Shigekazu Nagata

  • 1From the Department of Medical Chemistry, Graduate School of Medicine, Kyoto University, Yoshida, Sakyo-ku, Kyoto 606-8501, Japan and.

The Journal of Biological Chemistry
|January 31, 2014
PubMed
Summary

Transmembrane proteins TMEM16A and TMEM16F form homodimers and share similar mechanisms for plasma membrane localization and stability. However, their pore regions dictate distinct functions in calcium-dependent chloride transport and phospholipid scrambling.

Keywords:
Chloride ChannelsEnzyme MutationPhosphatidylserinePlasma MembraneProtein Domains

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Area of Science:

  • Molecular and Cellular Biology
  • Membrane Protein Function
  • Ion Transport and Lipid Dynamics

Background:

  • TMEM16A facilitates calcium-dependent chloride (Cl-) transport.
  • TMEM16F mediates calcium-dependent phospholipid scrambling.
  • Both are eight-transmembrane domain proteins with cytoplasmic termini.

Purpose of the Study:

  • To investigate the functional similarities and differences between TMEM16A and TMEM16F.
  • To elucidate the roles of protein domains in membrane localization, stability, and activity.
  • To identify potential inhibitors for these protein functions.

Main Methods:

  • Established cell-based assay systems for Cl- channel and phospholipid scramblase activity.
  • Utilized chemical cross-linking to assess protein dimerization.
  • Performed deletion and swapping analyses of protein termini and pore regions.
  • Investigated the effects of specific chemical inhibitors.

Main Results:

  • TMEM16A and TMEM16F form homodimers.
  • Cytoplasmic N- and C-terminal regions are crucial for plasma membrane localization and stability, respectively, and are exchangeable.
  • The pore region is essential for both Cl- channel and scramblase activities.
  • Specific chemicals differentially inhibit TMEM16A and TMEM16F activities.

Conclusions:

  • TMEM16A and TMEM16F share conserved mechanisms for membrane targeting and stabilization.
  • Distinct pore regions account for their specialized functions.
  • Differential inhibition suggests therapeutic potential for targeting these proteins.