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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Structure of Porins01:21

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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
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The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

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The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
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Protein Transport into the Inner Mitochondrial Membrane01:34

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Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
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Related Experiment Video

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Reconstitution of Msp1 Extraction Activity with Fully Purified Components
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Structure and function of TMEM16 proteins (anoctamins).

Nicoletta Pedemonte, Luis J V Galietta

    Physiological Reviews
    |April 3, 2014
    PubMed
    Summary

    Transmembrane protein 16 (TMEM16) family members, anoctamins, are crucial for ion transport and lipid scrambling. Some TMEM16 proteins, like TMEM16A, evolved specialized ion channel functions, while others retain dual roles.

    Area of Science:

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

    Background:

    • Transmembrane protein 16 (TMEM16) family, also known as anoctamins, perform diverse cellular roles including ion transport and phospholipid scrambling.
    • TMEM16A (anoctamin-1) and TMEM16B (anoctamin-2) function as calcium-activated chloride channels (CaCCs), vital for physiological processes like epithelial transport and muscle contraction.
    • Genetic studies in mice reveal TMEM16A's critical role in epithelial secretion and gastrointestinal motility.

    Purpose of the Study:

    • To elucidate the multifaceted functions of the TMEM16 protein family.
    • To investigate the evolutionary divergence of TMEM16 proteins towards specialized or dual functional roles.
    • To explore the link between anoctamin gene mutations and associated human genetic diseases.

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    Main Methods:

    • Review of existing literature on TMEM16 protein functions, including ion channel activity and lipid scrambling.
    • Analysis of genetic ablation studies in model organisms (e.g., mice).
    • Examination of structure-function relationships and evolutionary conservation across different TMEM16 members.

    Main Results:

    • TMEM16A and TMEM16B primarily function as CaCCs, essential for numerous physiological processes.
    • Other TMEM16 members, such as TMEM16F (anoctamin-6), exhibit significant phospholipid scramblase activity and can function as ion channels under specific conditions.
    • A TMEM16 protein from Aspergillus fumigatus demonstrates both ion channel and lipid scramblase activities, suggesting these dual functions are ancestral.

    Conclusions:

    • The TMEM16 family displays a spectrum of functions, from pure ion channels to proteins with dual ion transport and lipid scrambling capabilities.
    • Evolutionary pressures have likely led to specialization in some TMEM16 members, while others retain ancestral dual functions.
    • Dysfunctional TMEM16 proteins, due to mutations, are implicated in various genetic disorders, highlighting their importance in cellular homeostasis.