Beclin–phosphatidylinositol 3‐kinase complex functions at the trans‐Golgi network

By A. Kihara, Y. Kabeya, Y. Ohsumi, T. Yoshimori. EMBO Reports, 2001

868 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Physiology

View Paper: https://www.semanticscholar.org/paper/ecb346e548d584ca05fd56417b67a52500f2f7eb

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. N. Mizushima
2. D. Klionsky
3. Beth Levine
4. V. Deretic
5. I. Slaninová
6. Guido Kroemer
7. T. Yoshimori
8. S. Tooze

In Epidemiology

1. Beth Levine
2. N. Mizushima
3. D. Klionsky
4. Guido Kroemer
5. I. Slaninová
6. V. Deretic
7. T. Yoshimori
8. Douglas R. Green

In Physiology

1. N. Mizushima
2. Beth Levine
3. Guido Kroemer
4. I. Slaninová
5. V. Deretic
6. D. Klionsky
7. T. Yoshimori
8. S. Tooze

Citations in the corpus

• Inhibition of Macroautophagy Triggers Apoptosis (2005, background): “Beclin 1 localizes to the trans-Golgi network, belongs to the class III phosphatidylinositol 3-kinase complex, and participates in autophagosome formation (33, 45).”
• Autophagy as a cell death and tumor suppressor mechanism (2004, background): “Nevertheless, the localization of Beclin 1/PI 3-kinase to the trans-Golgi network in mammalian cells suggests that this compartment may be important in mammalian autophagic vesicle formation (Kihara et al., 2001a).”
• LC3 conjugation system in mammalian autophagy (2004, background): “In contrast to the class 3 PI3kinase, whose activity is essential to autophagy (Ogier-Denis & Codogno, 2003; Kihara et al., 2001), the class 1 PI3 kinase strongly inhibits autophagy (Arico et al., 2001).”
• Promotion of tumorigenesis by heterozygous disruption of the beclin 1 autophagy gene. (2003, neutral): “As part of a class III PI3K complex, Beclin 1 is thought to be important in mediating the localization of other autophagy proteins to pre-autophagosomal structures (20).”
• Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG. (2008, background): “Type 1 and 2 complexes function in autophagy and the vacuolar protein sorting pathway, respectively (Kihara et al., 2001b).”
• Autophagy gone awry in neurodegenerative diseases (2010, neutral): “Three proteins—Vps15, Vps34 and beclin-1—are essential components of this complex, and their recruitment to the phagophore initiates the nucleation proces”
• Autophagy gene-dependent clearance of apoptotic cells during embryonic development. (2007, background): “Beclin 1 is the mammalian ortholog of yeast Atg6 and interacts with Class III PI3K (Vps34) to mediate the localization of other autophagy proteins to the preautophagosomal membrane (Kihara et al., 2001; Liang et al., 1999).”
• Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium (2007, neutral): “beclin 1 mainly in the ER and mitochondria in colon cancer cells,(53) analysis of endogenous beclin in other cell types suggests that it resides in the trans-golgi network or in as yet uncharacterized cytosolic structures.(24,54) ER-localized Bcl-2 lowers the steady-state level of Ca2þ in the ER ([C”
• Molecular definitions of autophagy and related processes (2017, neutral): “Either mammalian phagophores or omegasomes, or both, stain positively for ULK1, ATG13, ATG101, FIP200, VPS34, BECN1, VPS15, ATG5, ATG12, ATG16L1, DFCP1 as well as for lipidated LC3 family members (Antonioli et al , 2016).”
• Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages (2009, background): “Beclin 1 binds to hVps34/class III phosphatidylinositol-3-kinase (PI(3)K) through its evolutionarily conserved domain (ECD”