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RSS FeedsIJMS, Vol. 22, Pages 12778: Folding and Insertion of Transmembrane Helices at the ER (International Journal of Molecular Sciences)

 
 

26 november 2021 08:49:03

 
IJMS, Vol. 22, Pages 12778: Folding and Insertion of Transmembrane Helices at the ER (International Journal of Molecular Sciences)
 


In eukaryotic cells, the endoplasmic reticulum (ER) is the entry point for newly synthesized proteins that are subsequently distributed to organelles of the endomembrane system. Some of these proteins are completely translocated into the lumen of the ER while others integrate stretches of amino acids into the greasy 30 Å wide interior of the ER membrane bilayer. It is generally accepted that to exist in this non-aqueous environment the majority of membrane integrated amino acids are primarily non-polar/hydrophobic and adopt an α-helical conformation. These stretches are typically around 20 amino acids long and are known as transmembrane (TM) helices. In this review, we will consider how transmembrane helices achieve membrane integration. We will address questions such as: Where do the stretches of amino acids fold into a helical conformation? What is/are the route/routes that these stretches take from synthesis at the ribosome to integration through the ER translocon? How do these stretches ‘know’ to integrate and in which orientation? How do marginally hydrophobic stretches of amino acids integrate and survive as transmembrane helices?


 
38 viewsCategory: Biochemistry, Biophysics, Molecular Biology
 
IJMS, Vol. 22, Pages 12776: 3D Structures of IgA, IgM, and Components (International Journal of Molecular Sciences)
IJMS, Vol. 22, Pages 12775: Deficiency of T-Cell Intracellular Antigen 1 in Murine Embryonic Fibroblasts Is Associated with Changes in Mitochondrial Morphology and Respiration (International Journal of Molecular Sciences)
 
 
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