C
Christopher A. Lamb
Researcher at London Research Institute
Publications - 19
Citations - 2078
Christopher A. Lamb is an academic researcher from London Research Institute. The author has contributed to research in topics: Autophagy & Autophagosome. The author has an hindex of 10, co-authored 19 publications receiving 1803 citations. Previous affiliations of Christopher A. Lamb include Francis Crick Institute & University of Glasgow.
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Journal ArticleDOI
The autophagosome: origins unknown, biogenesis complex
TL;DR: It is proposed that the isolation membrane forms from the mitochondria-associated endoplasmic reticulum (ER) membrane (MAM) and the role of ATG proteins and the vesicular trafficking machinery in autophagosome formation is proposed.
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TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes
Andrea Longatti,Christopher A. Lamb,Minoo Razi,Shin-ichiro Yoshimura,Francis A. Barr,Sharon A. Tooze +5 more
TL;DR: The noncatalytic RabGAP protein TBC1D14 regulates the Rab11- and ULK1-positive recycling endosomes required for autophagosome formation upon starvation.
Journal ArticleDOI
Endocytosis and autophagy: Shared machinery for degradation.
TL;DR: Recent findings highlighting the role of the classical endosomal pathway, from plasma membrane to lysosome, in the formation and expansion of the phagophore and subsequent degradation of the autophagosome contents are discussed.
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TBC1D14 regulates autophagy via the TRAPP complex and ATG9 traffic
Christopher A. Lamb,Stefanie Nühlen,Delphine Judith,David Frith,Ambrosius P. Snijders,Christian Behrends,Sharon A. Tooze +6 more
TL;DR: A model whereby TBC1D14 and TRAPPIII regulate a constitutive trafficking step from peripheral recycling endosomes to the early Golgi, maintaining the cycling pool of ATG9 required for initiation of autophagy is proposed.
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BIMEL, an intrinsically disordered protein, is degraded by 20S proteasomes in the absence of poly-ubiquitylation
Ceri M. Wiggins,Peter Tsvetkov,Mark Johnson,Claire L. Joyce,Christopher A. Lamb,Nia J. Bryant,David Komander,Yosef Shaul,Simon J. Cook +8 more
TL;DR: It is shown that BIMEL is degraded by isolated 20S proteasomes but that this is prevented when BIMels is bound to its pro-survival target protein MCL-1, and a novel ubiquitin-independent pathway for the proteasome-dependent destruction of this highly toxic protein is defined.