Generally over 90% of all membrane phosphatidyl serine (PS) is found on the inner monolayers of the cell membrane. Which of the following explains this phenomenon ?
-the movement of phospholipids frol one monolayer to another is a very slow reaction despite the fact that it works with the concentration gradient
-under normal condotions within the cell, the activity of scramblase enzymes is relatively low and thus does not allow for movement between monolayers

Question

24-11-2022
Biology

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Generally over 90% of all membrane phosphatidyl serine (PS) is found on the inner monolayers of the cell membrane. Which of the following explains this phenomenon ?
-the movement of phospholipids frol one monolayer to another is a very slow reaction despite the fact that it works with the concentration gradient
-under normal condotions within the cell, the activity of scramblase enzymes is relatively low and thus does not allow for movement between monolayers

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rathipushpendra345 rathipushpendra345 · Answer 1 · 2022-11-29T09:35:41+01:00

Despite using concentration gradient, migration of phospholipids from one monolayer to another is relatively sluggish response. It is possible for phospholipids to migrate between bilayers without being catalyzed.

Monolayer movement is sluggish and cannot be depended upon to keep the asymmetry equilibrium. Instead, phospholipid transport across the bilayers is catalyzed by lipid translocator proteins. Phospholipids are transferred from the outside to the inner leaflet via flippases. Flippases primarily transport phosphatidylserine and to a lesser extent phosphatidylethanolamine to maintain the charge gradient across the membrane. Additionally, flippases facilitate the transfer of cholesterol from the intracellular to external monolayers.

Phospholipids, in particular the choline-derived phospholipids phospatidylcholine and sphingomyelin, are moved by flippases in the reverse direction. The majority of the time, ATP hydrolysis is required for these catalyzed motions. The scramblases are a third type of protein that interchange phospholipids between the two leaflets through a calcium-activated, ATP-independent mechanism.

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