4z88: Difference between revisions
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/JIP1_DROME JIP1_DROME]] The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (By similarity). | [[http://www.uniprot.org/uniprot/JIP1_DROME JIP1_DROME]] The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (By similarity). | ||
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== Publication Abstract from PubMed == | |||
Synaptic vesicles (SVs) fuse at active zones (AZs) covered by a protein scaffold, at Drosophila synapses comprised of ELKS family member Bruchpilot (BRP) and RIM-binding protein (RBP). We here demonstrate axonal co-transport of BRP and RBP using intravital live imaging, with both proteins co-accumulating in axonal aggregates of several transport mutants. RBP, via its C-terminal Src-homology 3 (SH3) domains, binds Aplip1/JIP1, a transport adaptor involved in kinesin-dependent SV transport. We show in atomic detail that RBP C-terminal SH3 domains bind a proline-rich (PxxP) motif of Aplip1/JIP1 with submicromolar affinity. Pointmutating this PxxP motif provoked formation of ectopic AZ-like structures at axonal membranes. Direct interactions between AZ proteins and transport adaptors seem to provide complex avidity and shield synaptic interaction surfaces of pre-assembled scaffold protein transport complexes, thus, favouring physiological synaptic AZ assembly over premature assembly at axonal membranes. | |||
A high affinity RIM-binding protein/Aplip1 interaction prevents the formation of ectopic axonal active zones.,Siebert M, Bohme MA, Driller JH, Babikir H, Mampell MM, Rey U, Ramesh N, Matkovic T, Holton N, Reddy-Alla S, Gottfert F, Kamin D, Quentin C, Klinedinst S, Andlauer TF, Hell SW, Collins CA, Wahl MC, Loll B, Sigrist SJ Elife. 2015 Aug 14;4. doi: 10.7554/eLife.06935. PMID:26274777<ref>PMID:26274777</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 10:21, 26 August 2015
SH3-II of Drosophila Rim-binding protein with Aplip1 peptideSH3-II of Drosophila Rim-binding protein with Aplip1 peptide
Structural highlights
Function[JIP1_DROME] The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (By similarity). Publication Abstract from PubMedSynaptic vesicles (SVs) fuse at active zones (AZs) covered by a protein scaffold, at Drosophila synapses comprised of ELKS family member Bruchpilot (BRP) and RIM-binding protein (RBP). We here demonstrate axonal co-transport of BRP and RBP using intravital live imaging, with both proteins co-accumulating in axonal aggregates of several transport mutants. RBP, via its C-terminal Src-homology 3 (SH3) domains, binds Aplip1/JIP1, a transport adaptor involved in kinesin-dependent SV transport. We show in atomic detail that RBP C-terminal SH3 domains bind a proline-rich (PxxP) motif of Aplip1/JIP1 with submicromolar affinity. Pointmutating this PxxP motif provoked formation of ectopic AZ-like structures at axonal membranes. Direct interactions between AZ proteins and transport adaptors seem to provide complex avidity and shield synaptic interaction surfaces of pre-assembled scaffold protein transport complexes, thus, favouring physiological synaptic AZ assembly over premature assembly at axonal membranes. A high affinity RIM-binding protein/Aplip1 interaction prevents the formation of ectopic axonal active zones.,Siebert M, Bohme MA, Driller JH, Babikir H, Mampell MM, Rey U, Ramesh N, Matkovic T, Holton N, Reddy-Alla S, Gottfert F, Kamin D, Quentin C, Klinedinst S, Andlauer TF, Hell SW, Collins CA, Wahl MC, Loll B, Sigrist SJ Elife. 2015 Aug 14;4. doi: 10.7554/eLife.06935. PMID:26274777[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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