The Golgi complex offers a unique possibility to search for the universal principles underlying biomembrane fission because a number of different biochemical pathways all lead to Golgi membrane fission: the CtBP3/BARS pathway (Weigert et al., 1999), the Gbeta-gamma-PKD pathway (Jamora et al., 1999; Liljedahl et al., 2001), and the MEK pathway (Acharya et al., 1998). Finally, dynamin, first discovered as a key player in endocytic fission, is likely to have a role in Golgi membrane fission as well (Cao et al., 2000). All of these machineries are composed of proteins. The role of lipids is less well understood.
The protein dynamin is a large GTPase regulating membrane constriction and fission during receptor-mediated endocytosis. Dynamin transforms liposomes containing anionic phospholipids into dynamin-coated tubules, and depending on their lipid composition, these tubules vesiculate upon addition of GTP (Sweitzer and Hinshaw, 1998). We observed that dynamin is a membrane-active molecule capable of penetrating in between the headgroups and, possibly, even into the acyl chain region of membrane lipids, and that lipid penetration is strongly stimulated by PA (Burger et al., 2000). These data suggest that dynamin-dependent membrane fission in vivo, may result from a local change in lipid composition followed by deep penetration of dynamin into the membrane, membrane destabilization and fission.
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Speculative Models
for biomembrane fission. For details see Burger (2000) Greasing membrane fusion and
fission machineries. Traffic 1:605-613. |
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References
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Burger, K.N.J. 2000. Greasing membrane fusion and
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Burger, K.N.J., R.A. Demel, S.L. Schmid, and B. de Kruijff. 2000. Dynamin is membrane-active: lipid insertion is induced by phosphoinositides and phosphatidic acid. Biochemistry 39:12485-12493.
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