By Herwig J. Hilderson, Stephen Fuller
Membrane fusion and concentrating on tactics are tightly regulated and coordinated. Dozens of proteins, originating from either the cytoplasm and membranes are concerned. the invention of homologous proteins from yeast to neurons validates a unified view. even though a lot is understood concerning the interfering proteins, the occasions taking place while lipid bilayers really fuse are much less transparent. It can be remembered that lipid bilayers behave like soap-bubbles fusing whilst assembly one another. during this appreciate interfering proteins might be regarded as fighting bad and pointless fusion and at last directing the organic membrane fusion strategy (when, the place, how, and overcoming the activation energy). during this most modern quantity within the well known Subcellular Biochemistry sequence, a few points of fusion of organic membranes in addition to similar difficulties are awarded. even supposing no longer entire, there's a lot of modern info together with on virus-induced membrane fusion. The members of the chapters are all one of the researchers who played a few of the pioneering reports within the box.
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Additional resources for Fusion of Biological Membranes and Related Problems
1997). 1). The model that subunits of coatomer might bind to the open effector site in the ARF1-ARFGAP complex is in agreement with the positions in ARF of amino acids residues shown to interact with coatomer (see above). Another interaction predicted for COPI assembly would be binding of the coat components to proteins present in the target membrane. 1). Using a photocrosslinking approach, the γ-subunit of coatomer has been identified as the direct binding partner of the cytoplasmic tail peptide of p23 (Harter and Wieland, 1998).
This led to the suggestion that a tripartite complex of ARF1, ARFGAP and coatomer exists on the surface of a membrane (Goldberg, 1999). A role of coatomer as effector for efficient GTP hydrolysis fits to the finding that in the ARF1-ARFGAP complex the effector site is open, and therefore accessible to coatomer (Goldberg, 1999). Resolution of the structure of this ternary complex will help to learn how ARF and coatomer work together in COPI vesicle formation. 3. Sorting at the trans -Golgi Network Along their route through the Golgi, secretory and membrane proteins destined for various post-Golgi pathways are intermixed.
1997). , 1993). , 1995). After a short release from a 15°C block, VSV-G is trapped in COPI vesicles. , 1995), and (v) several mutants of S. , 1992). 1. , 1991b). , 1991) (Table 1). ARF1, like Sar1p of the COPII coat, belongs to the family of Ras GTPases. , 1993) (COP for coat protein). Each subunit seems to be present in a stoichiometric ratio of one by one in both the cytosolic form of coatomer as well as in its membrane-associated form. , 1993). The function of monomeric ζ-COP is unknown. , 1993).