- picture Membrane traffic in eukaryotic cells

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- picture Membrane traffic in eukaryotic cells
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bet | 5/13 | Sana | 16.05.2024 | Hajmi | 1,48 Mb. | | #237391 |
Bog'liq Structure and function of biological membranes.2.2. 3- picture Membrane traffic in eukaryotic cells.
Distribution of lipids
The inner and outer leaflets of bilayers differ in their lipid composition. In mammalian cells, the outer leaflet of the plasma membrane contains predominantly PC and sphingomyelin, whereas PS and PE are found on the inner leaflet. During programmed cell death (apoptosis), PS is no longer restricted to the inner leaflet of the plasma membrane. It is exposed on the outer leaflet by the action of an enzyme called scramblase which is a type of flippase enzyme. PS is negatively charged, unlike PC, which has no net charge. The movement of PS into the outer leaflet therefore changes the charge of the plasma membrane as viewed from the outside of the cell. This change in surface charge labels the apoptotic cell for phagocytosis by phagocytic cells such as macrophages.
Lipid composition also varies between the organelles within eukaryotic cells. Cholesterol is synthesized in the ER, but the ER membrane has a relatively low cholesterol content, as much of the cholesterol is transported to other cellular membranes. The prevalence of cholesterol in membranes increases through the secretory pathway, with more in the Golgi than in the ER (the trans-Golgi network is richer in cholesterol than the cis-Golgi), and most in the plasma membrane. This increase in cholesterol through the secretory pathway results in slightly thicker membranes in the late Golgi and plasma membrane compared with the ER, and is thought to be a contributing factor to protein sorting through the pathway, as membrane proteins in the plasma membrane generally have longer hydrophobic transmembrane domains than membrane proteins that reside in the ER.
2.2. Synthesis of membrane proteins.
Membrane proteins
Membrane proteins are the nanomachines that enable membranes to send and receive messages and to transport molecules into and out of cells and compartments. Without membrane proteins the phospholipid membrane would present an impenetrable barrier and cells would be unable to communicate with their neighbours, transport nutrients into the cell or waste products out of it, or respond to external stimuli. Both unicellular and multicellular organisms need membrane proteins in order to live. The membrane proteins that are present in a particular membrane determine the substances to which it will be permeable and what signal molecules it can recognize.
Synthesis of membrane proteins
In eukaryotic cells, the synthesis of membrane proteins destined for the plasma membrane, ER or any other membrane-bound compartment begins on cytosolic ribosomes. After a short segment of protein has been synthesized, the ribosome, mRNA and nascent protein chain associate with the ER, where the rest of the protein is made and simultaneously inserted into the membrane. This phenomenon was first explained by Günter Blobel, David Sabatini and Bernhard Dobberstein in the 1970s. These scientists proposed that there is a ‘binding factor’ which recognizes the emerging protein chain and can dock the ribosome at the ER membrane. We now know that there is an N-terminal signal sequence within membrane proteins. These signal sequences are not identical but share a common motif, namely a hydrophobic stretch of 20–30 amino acids, a basic region at the N-terminus and a polar domain at the C-terminus of the signal. These N-terminal signal sequences are recognized by the signal recognition particle (SRP), which has binding sites for the signal sequence, ribosome and the SRP receptor which is embedded in the ER membrane. Upon binding the SRP, the ribosome pauses protein synthesis. The SRP binds to the SRP receptor, adjacent to a translocon pore in the ER membrane. The translocon is a protein pore through which membrane protein chains can be threaded into the membrane. It has a laterally opening gate to allow newly synthesized proteins into the ER membrane. Once the ribosome is at the translocon, the SRP dissociates and protein synthesis resumes.
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