SH3GLB, a New Endophilin-Related Protein Family Featuring an SH3 Domain

Pierrat, Benoı̂t; Simonen, Mika; Cueto, Maria; Mestan, Jürgen; Ferrigno, Paul Ko; Heim, Jutta

doi:10.1006/geno.2000.6378

Cited by 101 publications

(121 citation statements)

References 47 publications

Supporting

Mentioning

118

Contrasting

Order By: Relevance

“…15,16 In addition to its role in Bax activation and apoptosis, Bif-1 has been shown to function in the regulation of autophagy and intracellular membrane dynamics. 17 Importantly, decreased Bif-1 expression is found in various types of human cancer including gastric, 18 colorectal, 19 prostate, 20 pancreatic, 21 invasive urinary bladder and gallbladder cancers, 22 and loss of Bif-1 promotes tumor development in mice.…”

Section: Suppression Of Bif-1 Delays Egfr Endocytic Trafficking and Dmentioning

confidence: 99%

Bif-1 suppresses breast cancer cell migration by promoting EGFR endocytic degradation

Runkle

Meyerkord

Desai

et al. 2012

Cancer Biology & Therapy

View full text Add to dashboard Cite

Section: Suppression Of Bif-1 Delays Egfr Endocytic Trafficking and Dmentioning

confidence: 99%

Bif-1 suppresses breast cancer cell migration by promoting EGFR endocytic degradation

Runkle

Meyerkord

Desai

et al. 2012

Cancer Biology & Therapy

View full text Add to dashboard Cite

“…More recently, downregulation of the mitochondrial membrane bound fission protein, Fis1, could prevent mitochondrial fission and cell death [57]. Another protein involved in fission, Endophilin B1, was shown to translocate to the mitochondria during cell death and is required for the activation of Bax on the mitochondria, likely due to their direct interactions on the membrane during cell death [55,65]. Finally, knockdown of DAP3, a matrix protein shown to induce mitochondrial fission during cell death could inhibit fission and protect cells against apoptosis [48].…”

Section: What Is the Role Of Mitochondrial Fission In Cell Death?mentioning

confidence: 99%

“…Inhibition of Fis1, however, has been shown to disrupt Bax translocation and its activation at the mitochondria, which places these fusion proteins upstream of Drp1, at least within the apoptotic program [57]. It is possible that Endophilin B1, a Bax interactor during apoptosis, participates in the co-localization of Drp1 and Bax at the mitochondria during apoptosis, since Endophilin B1 is redistributed to mitochondria after cell death induction [55], although Endophilin B1 interacts with Bax mainly in the cytosol and does not significantly influence Bax mediated cell death [65]. Other proapoptotic factors, therefore, may be recruited to the mitochondrial to drive apoptosis facilitated by the fission machinery.…”

Section: What Is the Role Of Mitochondrial Fission In Cell Death?mentioning

confidence: 99%

Mitochondrial dynamics in the regulation of neuronal cell death

2007

View full text Add to dashboard Cite

Mitochondria undergo continuous fission and fusion events in physiological situations. Fragmentation of mitochondria during cell death has been shown to play a key role in cell death progression, including release of the mitochondrial apoptotic proteins. Ultrastructural changes in mitochondria, such as cristae remodeling, is also involved in cell death initiation. Here, we emphasize the important role of mitochondrial fission/fusion machinery in neuronal cell death. Unlike many other cell types such as immortalized cell lines, neurons are distinct morphologically and functionally. We will discuss how this uniqueness presents special challenges in the cellular response to neurotoxic stresses, and how this affects the mitochondrial dynamics in the regulation of cell death in neurons.

show abstract

“…In contrast, the physiological function of the Endophilin B family of proteins is not fully understood. Bif-1, also known as SH3GLB1 or Endophilin B1, was originally discovered as a Bax-binding protein 16,17 . Although Bif-1 has liposome tubulation activity in vitro, it appears as though this protein does not localize to transferrinpositive endosomes 18 .…”

mentioning

confidence: 99%

Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis

et al. 2007

View full text Add to dashboard Cite

Autophagy is an evolutionally conserved "self-eating" process. Although the genes essential for autophagy (termed Atg) have been identified in yeast, the molecular mechanism of how these Atg proteins control autophagosome formation in mammalian cells remains to be elucidated. Here, we demonstrate that Bif-1 (also known as Endophilin B1) interacts with Beclin 1 through UVRAG and acts as a positive mediator of the class III PI3-kinase (PI3KC3). In response to nutrition deprivation, Bif-1 localizes to autophagosomes where it colocalizes with Atg5, as well as LC3. Furthermore, loss of Bif-1 suppresses autophagosome formation. While the SH3 domain of Bif-1 is sufficient for binding to UVRAG, both the BAR and SH3 domains are required for Bif-1 to activate PI3KC3 and induce autophagosome formation. We also found that Bif-1 ablation prolongs cell survival under nutrient starvation. Moreover, knockout of Bif-1 significantly enhances the development of spontaneous tumors in mice. These findings suggest that Bif-1 joins the UVRAG-Beclin 1 complex as a potential activator of autophagy and tumor suppressor.Autophagy is a tightly orchestrated intracellular process for bulk degradation of cytoplasmic proteins or organelles that appears to be essential for many physiological processes such as cellular homeostasis, development, differentiation, tissue remodeling, cell survival and death, innate immunity, and pathogenesis in various organisms 1-4 . The process of autophagic degradation is initiated when a portion of the cytosolic components are sequestered in cupshaped membrane structures called isolation membranes 1, 2, 5, 6 . The isolation membranes are elongated and eventually sealed to become double-membrane vesicles called autophagosomes, which are then fused with lysosomes resulting in degradation of the enclosed components. Eighteen autophagy-related (Atg) genes have been characterized in S. cerevisiae and can be categorized into four functional groups: (1) the Atg1 protein kinase complex regulating the induction of autophagy, (2) the class III PI3-kinase (PI3KC3) lipid kinase complex controlling vesicle nucleation, (3) the Atg12-Atg5 and Atg8-phosphatidylethanolamine conjugation pathways for vesicle expansion and completion, and (4) the Atg protein retrieval system 2, 7 . Beclin 1, the mammalian homologue of yeast Atg6, is a key component of the PI3KC3 complex, which plays an essential role in autophagosome formation 8-11 . Although the phosphatidylinositol 3-phosphate (PtdIns-3-P) generated by PI3KC3 has been proposed to control membrane dynamics during autophagosome formation 3 , the molecular mechanism underlying this process remains unknown. Results Loss of Bif-1 suppresses caspase-independent cell deathWe have previously reported that Bif-1 localizes to mitochondria and regulates the activation of Bax and Bak during apoptosis induced by intrinsic death stimuli 21 . To examine Bif-1 localization in mouse embryonic fibroblast (MEF) cells during serum deprivation, we added a pancaspase inhibitor, z-VAD-fmk, to ...

show abstract

SH3GLB, a New Endophilin-Related Protein Family Featuring an SH3 Domain

Cited by 101 publications

References 47 publications

Bif-1 suppresses breast cancer cell migration by promoting EGFR endocytic degradation

Bif-1 suppresses breast cancer cell migration by promoting EGFR endocytic degradation

Mitochondrial dynamics in the regulation of neuronal cell death

Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis

Contact Info

Product

Resources

About