The Bif-1-Dynamin 2 membrane fission machinery regulates Atg9-containing vesicle generation at the Rab11-positive reservoirs

Takahashi, Yoshinori; Tsotakos, Nikolaos; Liu, Ying; Young, Michelle; Serfass, Jacob M.; Tang, Zifan; Abraham, Thomas; Wang, Hong Gang

doi:10.18632/oncotarget.8028

Cited by 43 publications

(49 citation statements)

References 41 publications

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“…This possibility was further supported by our finding that EndoB1 comoves with an integral membrane protein, the EGFR, and by a very recent report showing that Dyn2 and EndoB1 cooperate in the formation of vesicles containing Atg9, an integral membrane component of the autophagic pathway (57). The EGFR is a classic marker of biosynthetic and endocytic membrane trafficking pathways.…”

Section: Discussionsupporting

confidence: 73%

Association of Endophilin B1 with Cytoplasmic Vesicles

Baryłko

Mueller

et al. 2017

Biophysical Journal

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Endophilins are SH3-and BAR domain-containing proteins implicated in membrane remodeling and vesicle formation. Endophilins A1 and A2 promote the budding of endocytic vesicles from the plasma membrane, whereas endophilin B1 has been implicated in vesicle budding from intracellular organelles, including the trans-Golgi network and late endosomes. We previously reported that endophilins A1 and A2 exist almost exclusively as soluble dimers in the cytosol. Here, we present results of fluorescence fluctuation spectroscopy analyses indicating that, in contrast, the majority of endophilin B1 is present in multiple copies on small, highly mobile cytoplasmic vesicles. Formation of these vesicles was enhanced by overexpression of wild-type dynamin 2, but suppressed by expression of a catalytically inactive dynamin 2 mutant. Using dual-color heterospecies partition analysis, we identified the epidermal growth factor receptor on endophilin B1 vesicles. Moreover, a proportion of endophilin B1 vesicles also contained caveolin, whereas clathrin was almost undetectable on those vesicles. These results raise the possibility that endophilin B1 participates in dynamin 2-dependent formation of a population of transport vesicles distinct from those generated by A-type endophilins.

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Section: Discussionsupporting

confidence: 73%

Association of Endophilin B1 with Cytoplasmic Vesicles

Baryłko

Mueller

et al. 2017

Biophysical Journal

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“…This role is consistent with the general paradigm of BAR-containing proteins regulating fission events at vesicle biogenesis sites. Fission also requires the interaction between Bif-1 and Dynamin-2 through sequences outside of the N-BAR 44 . Bif-1 may remain on these vesicles as time-lapse microscopy suggests colocalization of Bif-1 and Atg9 (and possibly fusion of independent vesicles) 45 .…”

Section: Curvature Sensing Proteins In Autophagymentioning

confidence: 99%

Sensing Membrane Curvature in Macroautophagy

Nguyen

Shteyn

Melia

2017

Journal of Molecular Biology

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In response to intracellular stress events ranging from starvation to pathogen invasion, the cell activates one or more forms of macroautophagy. The key event in these related pathways is the de novo formation of a new organelle called the autophagosome, which surrounds and sequesters either random portions of the cytoplasm or selectively targets individual intracellular challenges. Thus the autophagosome is a flexible membrane platform with dimensions that ultimately depend upon the target cargo. The intermediate membrane, termed the phagophore or isolation membrane, is a cup-like structure with a clear concave face and a highly curved rim. The phagophore is largely devoid of integral membrane proteins, thus its shape and size are governed by peripherally-associated membrane proteins and possibly by the lipid composition of the membrane itself. Growth along the phagophore rim marks the progress of both organelle expansion and ultimately of organelle closure around a particular cargo. These two properties, a reliance on peripheral membrane proteins and a structurally-distinct membrane architecture, suggest that the ability to target or manipulate membrane curvature might be an essential activity of proteins functioning in this pathway. In this review, we discuss the extent to which membranes are naturally curved at each of the cellular sites believed to engage in autophagosome formation, review basic mechanisms used to sense this curvature and then summarize the existing literature concerning which autophagy proteins are capable of curvature recognition.

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“…mATG9 has been reported to form tubular-vesicular clusters from perinuclear RAB11-positive recycling endosomes. Tubulation of RAB11 recycling endosomes is induced upon nutrient deprivation and is dependent on the curvature inducing protein Bif-1 and dynamin 2 (Takahashi et al, 2016). mATG9 tubular-vesicular clusters are ultimately recruited adjacent to sites of autophagosome formation (Orsi et al, 2012), and this recruitment is independent of Ulk1 (Orsi et al, 2012) (Figure 3, right).…”

Section: Golgi/endosome/plasma Membranementioning

confidence: 99%

Crosstalk between the Secretory and Autophagy Pathways Regulates Autophagosome Formation

2017

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The induction of autophagy by nutrient deprivation leads to a rapid increase in the formation of autophagosomes, unique organelles that replenish the cellular pool of nutrients by sequestering cytoplasmic material for degradation. The urgent need for membrane to form autophagosomes during starvation, to maintain homeostasis, leads to a dramatic rearrangement of intracellular membranes. Here we discuss recent findings that have begun to uncover how different parts of the secretory pathway directly and indirectly contribute to autophagosome formation during starvation.

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The Bif-1-Dynamin 2 membrane fission machinery regulates Atg9-containing vesicle generation at the Rab11-positive reservoirs

Cited by 43 publications

References 41 publications

Association of Endophilin B1 with Cytoplasmic Vesicles

Association of Endophilin B1 with Cytoplasmic Vesicles

Sensing Membrane Curvature in Macroautophagy

Crosstalk between the Secretory and Autophagy Pathways Regulates Autophagosome Formation

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