Rab GTPases at a glance

Schwartz, Samantha L.; Cao, Canhong; Pylypenko, Olena; Rak, Alexey; Wandinger-Ness, Angela

doi:10.1242/jcs.03495

Cited by 31 publications

(24 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Rab GTPases are members of the Ras GTPase superfamily and are known to regulate four steps in membrane trafficking: vesicle formation, trafficking, tethering and fusion with target organelles. Almost 70 different Rab GTPases have been identified to date in mammalian cells [46]. Several of these have been found on exosomes, including Rab5, Rab11, Rab27 and Rab35.…”

Section: Exosome Biogenesismentioning

confidence: 99%

Exosomes and other extracellular vesicles in host–pathogen interactions

et al. 2014

View full text Add to dashboard Cite

An effective immune response requires the engagement of host receptors by pathogen-derived molecules and the stimulation of an appropriate cellular response. Therefore, a crucial factor in our ability to control an infection is the accessibility of our immune cells to the foreign material. Exosomes-which are extracellular vesicles that function in intercellular communication-may play a key role in the dissemination of pathogen-as well as host-derived molecules during infection. In this review, we highlight the composition and function of exosomes and other extracellular vesicles produced during viral, parasitic, fungal and bacterial infections and describe how these vesicles could function to either promote or inhibit host immunity.

show abstract

Section: Exosome Biogenesismentioning

confidence: 99%

Exosomes and other extracellular vesicles in host–pathogen interactions

et al. 2014

View full text Add to dashboard Cite

show abstract

“…Several proteins genetically linked to TDP-43 pathology play important roles in the endolysosomal pathway, which consists of different vesicle pools distinguishable by specific RAB-GTPases that regulate vesicle transport. The key compartments are RAB5positive early endosomes, RAB11-positive recycling endosomes, and RAB7-positive late endosomes/lysosomes (Schwartz et al, 2007). In addition, RAB4-positive endosomes allow faster recycling to the plasma membrane by skipping the endosomal recycling compartment critical for RAB11-dependent recycling (Sonnichsen et al, 2000;Maxfield & McGraw, 2004).…”

Section: Introductionmentioning

confidence: 99%

TDP‐43 loss of function inhibits endosomal trafficking and alters trophic signaling in neurons

et al. 2016

View full text Add to dashboard Cite

Nuclear clearance of TDP‐43 into cytoplasmic aggregates is a key driver of neurodegeneration in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD), but the mechanisms are unclear. Here, we show that TDP‐43 knockdown specifically reduces the number and motility of RAB11‐positive recycling endosomes in dendrites, while TDP‐43 overexpression has the opposite effect. This is associated with delayed transferrin recycling in TDP‐43‐knockdown neurons and decreased β2‐transferrin levels in patient CSF. Whole proteome quantification identified the upregulation of the ESCRT component VPS4B upon TDP‐43 knockdown in neurons. Luciferase reporter assays and chromatin immunoprecipitation suggest that TDP‐43 represses VPS4B transcription. Preventing VPS4B upregulation or expression of its functional antagonist ALIX restores trafficking of recycling endosomes. Proteomic analysis revealed the broad reduction in surface expression of key receptors upon TDP‐43 knockdown, including ErbB4, the neuregulin 1 receptor. TDP‐43 knockdown delays the surface delivery of ErbB4. ErbB4 overexpression, but not neuregulin 1 stimulation, prevents dendrite loss upon TDP‐43 knockdown. Thus, impaired recycling of ErbB4 and other receptors to the cell surface may contribute to TDP‐43‐induced neurodegeneration by blocking trophic signaling.

show abstract

“…Rab GTPases cycle between active GTP-bound and inactive GDP-bound forms, in order to carrying out their functions (Schwartz et al, 2008). Such cycling is regulated by Rab-GDP-dissociation inhibitors (GDIs) (Shisheva et al, 1999), Rab-GTPase-activiting proteins (GAPs), and Rab-GTP exchange factors (GEFs) (van de Graaf et al, 2006), and it is possible to use single amino acid substitutions to generate mutant Rab proteins that are locked in the GTP-bound or GDP-bound state.…”

Section: Introductionmentioning

confidence: 99%

A Rab11a-enriched subapical membrane compartment regulates a cytoskeleton-dependent transcytotic pathway in secretory epithelial cells of the lacrimal gland

Edman

Kothawala

et al. 2011

Journal of Cell Science

View full text Add to dashboard Cite

SummaryDespite observations that the lacrimal gland has been identified as the principal source of dimeric immunoglobulin A (dIgA) in tears, the mechanism used by lacrimal gland acinar cells (LGACs) to transcytose dIgA produced by interstitial plasma cells is not wellcharacterized. This study identifies a transcytotic pathway in LGACs regulated by Rab11a for polymeric immunoglobulin receptor (pIgR) and dIgA. EGFP-tagged Rab11a expressed in primary LGACs labeled a unique membrane compartment of comparable localization to endogenous Rab11a beneath the apical plasma membrane. This compartment was enriched in pIgR and clearly distinct from the regulated secretory pathway. Comparison of dIgA uptake in LGACs expressing wild type and dominant negative EGFPRab11a showed that the rapid exocytosis of dIgA was inhibited in acini expressing the dominant-negative protein, which additionally redistributed subapical pIgR. The trafficking of EGFP-Rab11a-enriched vesicles was regulated by microtubule-based and myosin Vb motors at distinct steps. Our data suggest that Rab11a is a crucial regulator of dIgA trafficking in primary acinar secretory epithelial cells and further support a role for microtubules, cytoplasmic dynein, actin filaments and myosin Vb in the maintenance of the Rab11a compartment in this primary secretory epithelial cell.

show abstract

Rab GTPases at a glance

Cited by 31 publications

References 0 publications

Exosomes and other extracellular vesicles in host–pathogen interactions

Exosomes and other extracellular vesicles in host–pathogen interactions

TDP‐43 loss of function inhibits endosomal trafficking and alters trophic signaling in neurons

A Rab11a-enriched subapical membrane compartment regulates a cytoskeleton-dependent transcytotic pathway in secretory epithelial cells of the lacrimal gland

Contact Info

Product

Resources

About