Phospholipid Scramblases
نویسنده
چکیده
The distribution of phospholipid types between the two leaflets of a membrane bilayer is a controlled feature of membrane structure. One of the two membrane catalytic activities governing this distribution randomizes the composition of the two leaflets-the phospholipid scramblases. Two proteins (Xkr8 and TMEM16F) required for the activation of these activities have been identified. One of these proteins (TMEM16F) is quite clearly a scramblase itself and provides insight into the mechanism by which transbilayer phospholipid movement is facilitated.
منابع مشابه
Ca2+-dependent phospholipid scrambling by a reconstituted TMEM16 ion channel
Phospholipid (PL) scramblases disrupt the lipid asymmetry of the plasma membrane, externalizing phosphatidylserine to trigger blood coagulation and mark apoptotic cells. Recently, members of the TMEM16 family of Ca(2+)-gated channels have been shown to be involved in Ca(2+)-dependent scrambling. It is however controversial whether they are scramblases or channels regulating scrambling. Here we ...
متن کاملCalcium-dependent Phospholipid Scramblase Activity of TMEM16 Family Members*
Background: TMEM16A and 16B work as Cl-channel, while 16F works as phospholipid-scramblase. Function of other TMEM16 members is unknown. Results: Using TMEM16F cells, TMEM16C, 16D, 16F, 16G and 16J were shown to be lipid scramblases. Conclusion: Some TMEM16 members are divided into two Cl-channels and five lipid-scramblases. Significance: Learning biochemical function of TMEM16 family members i...
متن کاملCalcium-dependent phospholipid scramblase activity of TMEM16 protein family members.
BACKGROUND TMEM16A and 16B work as Cl(-) channel, whereas 16F works as phospholipid scramblase. The function of other TMEM16 members is unknown. RESULTS Using TMEM16F(-/-) cells, TMEM16C, 16D, 16F, 16G, and 16J were shown to be lipid scramblases. CONCLUSION Some TMEM16 members are divided into two Cl(-) channels and five lipid scramblases. SIGNIFICANCE Learning the biochemical function of...
متن کاملFacilitated phospholipid translocation in vesicles and nucleated cells using synthetic small molecule scramblases.
A series of 16 synthetic scramblase candidates were prepared from a tris(aminoethyl)amine (TREN) scaffold and evaluated for ability to facilitate translocation of fluorescent phospholipid probes across vesicle membranes and endogenous phosphatidylserine across the plasma membrane of nucleated cells. More than half of the compounds were found to greatly accelerate phospholipid translocation in v...
متن کاملN-terminal proline-rich domain is required for scrambling activity of human phospholipid scramblases.
Human phospholipid scramblase 1 (hPLSCR1), a type II integral class membrane protein, is known to mediate bidirectional scrambling of phospholipids in a Ca(2+)-dependent manner. hPLSCR2, a homolog of hPLSCR1 that lacks N-terminal proline-rich domain (PRD), did not show scramblase activity. We attribute this absence of scramblase activity of hPLSCR2 to the lack of N-terminal PRD. Hence to invest...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره 8 شماره
صفحات -
تاریخ انتشار 2015