Targeting of Polytopic Proteins to the Plasma Membrane
نویسندگان
چکیده
منابع مشابه
Targeting of polytopic proteins to the plasma membrane.
Most proteins in plant cells are synthesized on cytoplasmic ribosomes and later get transported to their proper place of action. For proteins that function in the endomembrane system, at the plasma membrane, or outside the cell, translation occurs at the endoplasmic reticulum, and the resulting proteins are later trafficked via vesicular transport from there to their final destination. Proper s...
متن کاملPolytopic Proteins: Preventing Aggregation in the Membrane
It has been proposed that the aggregation of nascent transmembrane segments of polytopic proteins is prevented by chaperones present in the endoplasmic reticulum membrane; now the first experimental support for this proposal has been reported.
متن کاملTransmembrane segments of nascent polytopic membrane proteins control cytosol/ER targeting during membrane integration
During cotranslational integration of a eukaryotic multispanning polytopic membrane protein (PMP), its hydrophilic loops are alternately directed to opposite sides of the ER membrane. Exposure of fluorescently labeled nascent PMP to the cytosol or ER lumen was detected by collisional quenching of its fluorescence by iodide ions localized in the cytosol or lumen. PMP loop exposure to the cytosol...
متن کاملBiogenesis of Polytopic Membrane Proteins: Membrane Segments Assemble within Translocation Channels prior to Membrane Integration
The initial steps in the biogenesis of membrane proteins parallel that of secretory proteins. The translocation of membrane proteins, however, must be interrupted prior to the complete traversal of the membrane. This is followed by their folding and integrating into the lipid bilayer. We have previously shown that as each latent transmembrane segment (TMS) in a polytopic membrane protein emerge...
متن کاملPromiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle
Protein insertion into the bacterial inner membrane is facilitated by SecYEG or YidC. Although SecYEG most likely constitutes the major integration site, small membrane proteins have been shown to integrate via YidC. We show that YidC can also integrate multispanning membrane proteins such as mannitol permease or TatC, which had been considered to be exclusively integrated by SecYEG. Only SecA-...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Plant Physiology
سال: 2014
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.114.247080