Differential expression of endophilin 1 and 2 dimers at central nervous system synapses.
Endophilin 1 is proposed to participate in synaptic vesicle biogenesis through SH3 domain- mediated interactions with the polyphosphoinositide phosphatase synaptojanin and the GTPase dynamin. Endophilin family members have also been identified as binding partners for a number of diverse cellular proteins. We define here the endophilin 1- binding site within synaptojanin 1 and show that this sequence independently and selectively purifies from brain extracts endophilin 1 and a closely related protein, endophilin 2. Endophilin 2, like endophilin 1, is highly expressed in brain, concentrated in nerve terminals, and found in complexes with synaptojanin and dynamin. Although a fraction of endophilins 1 and 2 coexist in the same complex, the distribution of these endophilin isoforms among central synapses only partially overlaps. Endophilins 1 and 2 are found predominantly as stable dimers through a predicted coiled-coil domain in their conserved NH2-terminal moiety. Dimerization may allow endophilins to link a number of different cellular targets to the endocytic machinery.[1]References
- Differential expression of endophilin 1 and 2 dimers at central nervous system synapses. Ringstad, N., Nemoto, Y., De Camilli, P. J. Biol. Chem. (2001) [Pubmed]
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