Exocytic and endocytic membrane trafficking in axon development

Tojima, Takuro; Kamiguchi, Hiroyuki

doi:10.1111/dgd.12218

Cited by 54 publications

(59 citation statements)

References 154 publications

(335 reference statements)

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“…Notably, DCC/SNAP-25 exocytosis is partially dependent on VAMP-7, a lysosomal V-SNARE (Winkle et al, 2014), suggesting a similar lysosomal membrane source is also used in neurons. Further, the exocyst complex is required for axon outgrowth (Tojima and Kamiguchi, 2015). Thus, the circuitry that directs membrane addition during axon outgrowth and AC invasion appears to be shared.…”

Section: Discussionmentioning

confidence: 99%

Cell Invasion In Vivo via Rapid Exocytosis of a Transient Lysosome-Derived Membrane Domain

et al. 2017

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Summary Invasive cells use small invadopodia to breach basement membrane (BM), a dense matrix that encases tissues. Following the breach, a large protrusion forms to clear a path for tissue entry by poorly understood mechanisms. Using RNAi screening for defects in C. elegans anchor cell (AC) invasion, we found that UNC-6(netrin)/UNC-40(DCC) signaling at the BM breach site directs exocytosis of lysosomes using the exocyst and SNARE SNAP-29 to form a large protrusion that invades vulval tissue. Live-cell imaging revealed that the protrusion is enriched in the matrix metalloprotease ZMP-1 and transiently expands AC volume more than 20%, displacing surrounding BM and vulval epithelium. Photobleaching and genetic perturbations showed that the BM receptor dystroglycan forms a membrane diffusion barrier at the neck of the protrusion that enables protrusion growth. Together these studies define a netrin dependent pathway that builds an invasive protrusion, an isolated lysosome-derived membrane structure specialized to breach tissue barriers.

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Section: Discussionmentioning

confidence: 99%

Cell Invasion In Vivo via Rapid Exocytosis of a Transient Lysosome-Derived Membrane Domain

et al. 2017

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“…In neurons, endocytosis is a key regulator of multiple processes in neurons including signal transduction, axonal motility, and remodeling of the dendritic spines/PSD (Steketee and Goldberg 2012; Cosker and Segal 2014; Tojima and Kamiguchi 2015). Shank2 plays an important role in organizing proteins at the PSD thereby regulating PSD structure and function.…”

Section: Discussionmentioning

confidence: 99%

Shank2 Regulates Renal Albumin Endocytosis

et al. 2015

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Albuminuria is a strong and independent predictor of kidney disease progression but the mechanisms of albumin handling by the kidney remain to be fully defined. Previous studies have shown that podocytes endocytose albumin. Here we demonstrate that Shank2, a large scaffolding protein originally identified at the neuronal postsynaptic density, is expressed in podocytes in vivo and in vitro and plays an important role in albumin endocytosis in podocytes. Knockdown of Shank2 in cultured human podocytes decreased albumin uptake, but the decrease was not statistically significant likely due to residual Shank2 still present in the knockdown podocytes. Complete knockout of Shank2 in podocytes significantly diminished albumin uptake in vitro. Shank2 knockout mice develop proteinuria by 8 weeks of age. To examine albumin handling in vivo in wild-type and Shank2 knockout mice we used multiphoton intravital imaging. While FITC-labeled albumin was rapidly seen in the renal tubules of wild-type mice after injection, little albumin was seen in the tubules of Shank2 knockout mice indicating dysregulated renal albumin trafficking in the Shank2 knockouts. We have previously found that caveolin-1 is required for albumin endocytosis in cultured podocytes. Shank2 knockout mice had significantly decreased expression and altered localization of caveolin-1 in podocytes suggesting that disruption of albumin endocytosis in Shank2 knockouts is mediated via caveolin-1. In summary, we have identified Shank2 as another component of the albumin endocytic pathway in podocytes.

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“…Axonal growth cones are highly motile structures involved in axon outgrowth and guidance (59,60). They comprise a central region enriched in microtubules and transport vesicles and a peripheral region with a high concentration of actin filaments that organize lamellipodia and filopodia.…”

Section: Borc-dependent Lysosome Transport Promotes Axonal Growth-conementioning

confidence: 99%

BORC/kinesin-1 ensemble drives polarized transport of lysosomes into the axon

Farı́as

Guardia

Pace

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

185

234

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The ability of lysosomes to move within the cytoplasm is important for many cellular functions. This ability is particularly critical in neurons, which comprise vast, highly differentiated domains such as the axon and dendrites. The mechanisms that control lysosome movement in these domains, however, remain poorly understood. Here we show that an ensemble of BORC, Arl8, SKIP, and kinesin-1, previously shown to mediate centrifugal transport of lysosomes in nonneuronal cells, specifically drives lysosome transport into the axon, and not the dendrites, in cultured rat hippocampal neurons. This transport is essential for maintenance of axonal growth-cone dynamics and autophagosome turnover. Our findings illustrate how a general mechanism for lysosome dispersal in nonneuronal cells is adapted to drive polarized transport in neurons, and emphasize the importance of this mechanism for critical axonal processes.

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Exocytic and endocytic membrane trafficking in axon development

Cited by 54 publications

References 154 publications

Cell Invasion In Vivo via Rapid Exocytosis of a Transient Lysosome-Derived Membrane Domain

Cell Invasion In Vivo via Rapid Exocytosis of a Transient Lysosome-Derived Membrane Domain

Shank2 Regulates Renal Albumin Endocytosis

BORC/kinesin-1 ensemble drives polarized transport of lysosomes into the axon

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