<i>Drosophila</i>Past1 is involved in endocytosis and is required for germline development and survival of the adult fly

Olswang-Kutz, Yael; Gertel, Yaron; Benjamin, Sigi; Sela, Orly; Pekar, Olga; Arama, Eli; Steller, Hermann; Horowitz, Mia; Segal, Daniel

doi:10.1242/jcs.038521

Cited by 27 publications

(48 citation statements)

References 57 publications

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“…However, a role for Numb in regulating post-endocytic trafficking in Drosophila has not yet been demonstrated. Genetic interaction between the Drosophila EHD orthologue Past1 and the Notch pathway has recently been reported, and we previously showed that Drosophila Numb interacts with Past1 (41,73). These observations suggest that Drosophila Numb is likely to have a similar postendocytic function.…”

Section: Discussionsupporting

confidence: 53%

Numb Regulates Post-endocytic Trafficking and Degradation of Notch1

McGill

Dho

Weinmaster

et al. 2009

Journal of Biological Chemistry

185

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Section: Discussionsupporting

confidence: 53%

Numb Regulates Post-endocytic Trafficking and Degradation of Notch1

McGill

Dho

Weinmaster

et al. 2009

Journal of Biological Chemistry

185

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“…1A). Therefore, as described in C. elegans ) and D. melanogaster (Olswang-Kutz et al, 2009), D. discoideum contains a single EHD protein, here referred to as EHD.…”

Section: Discoideum Contains a Single Ehd Protein With Endosomal Lmentioning

confidence: 99%

Dictyostelium EHD associates with Dynamin and participates in phagosome maturation

Gueho

Bosmani

Gopaldass

et al. 2016

Journal of Cell Science

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Proteins that contain Eps15 homology domains (EHDs) in their C-terminus are newly identified key regulators of endosomal membrane trafficking. Here, we show that D. discoideum contains a single EHD protein (referred to as EHD) that localizes to endosomal compartments and newly formed phagosomes. We provide the first evidence that EHD regulates phagosome maturation. Deletion of EHD results in defects in intraphagosomal proteolysis and acidification. These defects are linked to early delivery of lysosomal enzymes and fast retrieval of the vacuolar H + -ATPase in maturing phagosomes. We also demonstrate that EHD physically interacts with DymA. Our results indicate that EHD and DymA can associate independently with endomembranes, and yet they share identical kinetics in recruitment to phagosomes and release during phagosome maturation. Functional analysis of ehd − , dymA − and double dymA − ehd − knockout strains indicate that DymA and EHD play non-redundant and independent functions in phagosome maturation. Finally, we show that the absence of EHD leads to increased tubulation of endosomes, indicating that EHD participates in the scission of endosomal tubules, as reported for DymA.

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“…Dominant negative substitutions within RME-1, G81R and G429R, failed to recycle yolk receptors as well. The Drosophila EHD homolog, Past1, has also been implicated in endocytosis (Olswang-Kutz et al , 2009). Garland cells from Past1 mutants demonstrated a reduced ability to endocytose fluorescently labeled avidin.…”

Section: Ferlin Proteins In Cytoskeletal Rearrangements During Myomentioning

confidence: 99%

Ferlin Proteins in Myoblast Fusion and Muscle Growth

Posey¹,

Demonbreun²,

McNally³

2011

Current Topics in Developmental Biology

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Myoblast fusion contributes to muscle growth in development and during regeneration of mature muscle. Myoblasts fuse to each other as well as to multinucleate myotubes to enlarge the myofiber. The molecular mechanisms of myoblast fusion are incompletely understood. Adhesion, apposition, and membrane fusion are accompanied by cytoskeletal rearrangements. The ferlin family of proteins is implicated in human muscle disease and has been implicated in fusion events in muscle, including myoblast fusion, vesicle trafficking and membrane repair. Dysferlin was the first mammalian ferlin identified and it is now know that there are six different ferlins. Loss of function mutations in the dysferlin gene lead to limb girdle muscular dystrophy and the milder disorder Miyoshi myopathy. Dysferlin is a membrane-associated protein that has been implicated in resealing disruptions in the muscle plasma membrane. Newer data supports a broader role for dysferlin in intracellular vesicular movement, a process also important for resealing. Myoferlin is highly expressed in myoblasts that undergoing fusion, and the absence of myoferlin leads to impaired myoblast fusion. Myoferlin also regulates intracellular trafficking events, including endocytic recycling, a process where internalized vesicles are returned to the plasma membrane. The trafficking role of ferlin proteins is reviewed herein with a specific focus as to how this machinery alters myogenesis and muscle growth.

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DrosophilaPast1 is involved in endocytosis and is required for germline development and survival of the adult fly

Cited by 27 publications

References 57 publications

Numb Regulates Post-endocytic Trafficking and Degradation of Notch1

Numb Regulates Post-endocytic Trafficking and Degradation of Notch1

Dictyostelium EHD associates with Dynamin and participates in phagosome maturation

Ferlin Proteins in Myoblast Fusion and Muscle Growth

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