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J. Biol. Chem., Vol. 278, Issue 15, 13531-13538, April 11, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/15/13531    most recent M213205200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tani, K. Articles by Tagaya, M. Search for Related Content PubMed PubMed Citation Articles by Tani, K. Articles by Tagaya, M. Social Bookmarking                      What's this?

Mapping of Functional Domains of -SNAP^*

Katsuko Tani, Mika Shibata, Kazuho Kawase, Hoshiko Kawashima, Kiyotaka Hatsuzawa, Masami Nagahama, and Mitsuo Tagaya

From the School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan

-Soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (-SNAP) is capable of stabilizing a 20 S complex consisting of NSF, -SNAP, and SNAP receptors (SNAREs), but its function in vesicular transport is not fully understood. Our two-hybrid analysis revealed that -SNAP, unlike -SNAP, interacts directly with NSF, as well as Gaf-1/Rip11, but not with SNAREs. Gaf-1/Rip11 is a -SNAP-associated factor that belongs to the Rab11-interacting protein family. To gain insight into the molecular basis for the interactions of -SNAP with NSF and Gaf-1/Rip11, we determined the regions of the three proteins involved in protein-protein interactions. -SNAP bound to NSF via its extreme C-terminal region, and the full-length NSF was needed to interact with -SNAP. Both the N-terminal and C-terminal regions of -SNAP were required for the binding to Gaf-1/Rip11. Gaf-1/Rip11 bound to -SNAP via its C-terminal domain comprising a putative coiled-coil region. Although the C-terminal domain of Gaf-1/Rip11 also interacts with Rab11, the binding of -SNAP and Rab11 to Gaf-1/Rip11 was not mutually exclusive. Rather, Gaf-1/Rip11 was capable of serving a link between -SNAP and Rab11. A complex comprising -SNAP and Gaf-1/Rip11 was disassembled in a process coupled to NSF-mediated ATP hydrolysis, suggesting that the interaction between -SNAP and Gaf-1/Rip11 is of functional significance.

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