Adaptor protein complex-4 (AP-4) is expressed in the central nervous system neurons and interacts with glutamate receptor δ2

Yap, Chan Choo; Murate, Motohide; Kishigami, Satoshi; Muto, Yuko; Kishida, Haruo; Hashikawa, Tsutomu; Yano, Ryoji

doi:10.1016/s1044-7431(03)00164-7

Cited by 64 publications

(64 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…4). Adaptors other than AP-1B, possibly AP-4 (Yap et al, 2003), therefore could mediate somatodendritic targeting of YxxØ and GYSY somatodendritic signals. The FxNPxY motif, however, is a poor somatodendritic signal in neurons and apparently does not make efficient use of neuronal adaptor complexes.…”

Section: Mapping Of a Somatodendritic Targeting Signalmentioning

confidence: 99%

Pathway selection to the axon depends on multiple targeting signals in NgCAM

Yap

Nokes

Wisco

et al. 2008

Journal of Cell Science

View full text Add to dashboard Cite

Similar to most differentiated cells, both neurons and epithelial cells elaborate distinct plasma membrane domains that contain different membrane proteins. We have previously shown that the axonal cell-adhesion molecule L1/NgCAM accumulates on the axonal surface by an indirect transcytotic pathway via somatodendritic endosomes. MDCK epithelial cells similarly traffic NgCAM to the apical surface by transcytosis. In this study, we map the signals in NgCAM required for routing via the multi-step transcytotic pathway. We identify both a previously mapped tyrosine-based signal as a sufficient somatodendritic targeting signal, as well as a novel axonal targeting signal in the cytoplasmic tail of NgCAM. The axonal signal is glycine and serine rich, but only the glycine residues are required for activity. The somatodendritic signal is cis-dominant and needs to be inactivated in order for the axonal signal to be executed. Additionally, we show that the axonal cytoplasmic signal promotes apical targeting in MDCK cells. Transcytosis of NgCAM to the axon thus requires the sequential regulated execution of multiple targeting signals.

show abstract

Section: Mapping Of a Somatodendritic Targeting Signalmentioning

confidence: 99%

Pathway selection to the axon depends on multiple targeting signals in NgCAM

Yap

Nokes

Wisco

et al. 2008

Journal of Cell Science

View full text Add to dashboard Cite

show abstract

“…AP1 components ␥2 and 2, and AP2 components ␣2, 1, and 1 are strongly up-regulated in the immune lineages, whereas the AP3 components ␤2 and 2 are up-regulated in brain tissues, consistent with their known biochemical functions in the neurons (Hinners and Tooze, 2003; Figure 5). The AP4 components ⑀1 and 1 are up-regulated in neuronal ganglions and nodes, suggesting an enhanced function for AP4-mediated pathways in these tissues (Yap et al, 2003). AP complex clusters also include other components with which biochemical interactions have already been established (Lafer, 2002;Hinners and Tooze, 2003).…”

Section: Coat Machineriesmentioning

confidence: 99%

Large-Scale Profiling of Rab GTPase Trafficking Networks: The Membrome

Gürkan

Lapp

Alory

et al. 2005

MBoC

115

107

View full text Add to dashboard Cite

Rab GTPases and SNARE fusion proteins direct cargo trafficking through the exocytic and endocytic pathways of eukaryotic cells. We have used steady state mRNA expression profiling and computational hierarchical clustering methods to generate a global overview of the distribution of Rabs, SNAREs, and coat machinery components, as well as their respective adaptors, effectors, and regulators in 79 human and 61 mouse nonredundant tissues. We now show that this systems biology approach can be used to define building blocks for membrane trafficking based on Rab-centric protein activity hubs. These Rab-regulated hubs provide a framework for an integrated coding system, the membrome network, which regulates the dynamics of the specialized membrane architecture of differentiated cells. The distribution of Rab-regulated hubs illustrates a number of facets that guides the overall organization of subcellular compartments of cells and tissues through the activity of dynamic protein interaction networks. An interactive website for exploring datasets comprising components of the Rab-regulated hubs that define the membrome of different cell and organ systems in both human and mouse is available at http://www.membrome.org/. INTRODUCTIONUnderstanding the molecular basis for the organization of the exocytic and endocytic membrane trafficking pathways in the eukaryotic cell remains a formidable challenge. The foundation of these pathways is the lipid bilayer that separates different subcellular compartments, their distinguishing features encoded by phospholipid composition, and unique sets of integral and peripheral membrane proteins. By harnessing and regulating the fundamental processes of membrane fission and fusion through the action of protein complexes, the lipid bilayer can be exploited to produce a variety of distinct subcellular compartments with unique chemical environments that play essential roles in cell and organ function. Moreover, it is now evident that these subcellular compartments are dynamic structures in continuous and specific communication through carrier vesicles and tubules that mobilize cargo to specific destinations. They can be disassembled and reassembled in a remarkably facile manner in response to cell signaling pathways, mitosis, or by simple chemical perturbants.Implicit in these dynamic pathways is the need to systematically and reversibly regulate protein interactions. Although traditional phylogenetic analyses provided significant insights into the diversity of components that direct membrane traffic (Pereira-Leal and Seabra, 2000;Chen and Scheller, 2001;Pereira-Leal and Seabra, 2001), our understanding of the basic cellular building blocks that organize this diversity into contiguous pathways is still fragmentary. Reductionist approaches using biochemical and molecular tools also provide important insights into specific steps of a pathway. However, understanding the global interconnectivities of complex biological pathways, such as cargo trafficking, will require new approaches utilizing modern ...

show abstract

“…They include Rab8 (Huber et al, 1993a,b), KIFC2 (Saito et al, 1997), KIF17 (Setou et al, 2000;Guillaud et al, 2003), AP-1 (Eiraku et al, 2002), and AP-4 (Yap et al, 2003). At present, it remains unknown what molecule interacts with the cytoplasmic tail of TLCN.…”

Section: A Transgenic Mouse System For Analysis Of Polarized Targetinmentioning

confidence: 99%