scholarly journals PDCD6IP , encoding a regulator of the ESCRT complex, is mutated in microcephaly

2020 ◽  
Vol 98 (1) ◽  
pp. 80-85 ◽  
Author(s):  
Amjad Khan ◽  
Manal Alaamery ◽  
Salam Massadeh ◽  
Abdulrahman Obaid ◽  
Amna A. Kashgari ◽  
...  
Keyword(s):  
Escrt Complex

Heme acquisition by Shu1 requires Nbr1 and proteins of the ESCRT complex in Schizosaccharomyces pombe

2019 ◽  
Vol 112 (5) ◽  
pp. 1499-1518 ◽  
Author(s):  
Thierry Mourer ◽  
Ariane Brault ◽  
Simon Labbé
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Heme Acquisition ◽  
Escrt Complex

Author response for "PDCD6IP, encoding a regulator of the ESCRT complex, is mutated in microcephaly"

2020 ◽  
Author(s):  
Amjad Khan ◽  
Manal Alaamery ◽  
Salam Massadeh ◽  
Abdulrahman Obaid ◽  
Amna A. Kashgari ◽  
...  
Keyword(s):  
Author Response ◽  
Escrt Complex

scholarly journals Relationship of DFG16 to the Rim101p pH Response Pathway in Saccharomyces cerevisiae and Candida albicans

2005 ◽  
Vol 4 (5) ◽  
pp. 890-899 ◽  
Author(s):  
Karen J. Barwell ◽  
Jacob H. Boysen ◽  
Wenjie Xu ◽  
Aaron P. Mitchell
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Candida Albicans ◽  
Proteolytic Processing ◽  
Multivesicular Bodies ◽  
Ph Response ◽  
New Gene ◽  
Escrt Complex ◽  
Membrane Spanning ◽  
Relationship Of ◽  
G Protein Coupled

ABSTRACT Many fungal pH responses depend upon conserved Rim101p/PacC transcription factors, which are activated by C-terminal proteolytic processing. The means by which environmental pH is sensed by this pathway are not known. Here, we report a screen of the Saccharomyces cerevisiae viable deletion mutant library that has yielded a new gene required for processed Rim101p accumulation, DFG16. An S. cerevisiae dfg16Δ mutant expresses Rim101p-repressed genes at elevated levels. In addition, Candida albicans dfg16Δ/dfg16Δ mutants are defective in alkaline pH-induced filamentation, and their defect is suppressed by expression of truncated Rim101-405p. Thus, Dfg16p is a functionally conserved Rim101p pathway member. Many proteins required for processed Rim101p accumulation are members of the ESCRT complex, which functions in the formation of multivesicular bodies (MVBs). Staining with the dye FM4-64 indicates that the S. cerevisiae dfg16Δ mutant does not have an MVB defect. We find that two transcripts, PRY1 and ASN1, respond to mutations that affect both the Rim101p and MVB pathways but not to mutations that affect only one pathway. The S. cerevisiae dfg16Δ mutation does not affect PRY1 and ASN1 expression, thus confirming that Dfg16p function is restricted to the Rim101p pathway. Dfg16p is homologous to Aspergillus nidulans PalH, a component of the well-characterized PacC processing pathway. We verify that the previously recognized PalH homolog, Rim21p, also functions in the S. cerevisiae Rim101p pathway. Dfg16p is predicted to have seven membrane-spanning segments and a long hydrophilic C-terminal region, as expected if Dfg16p were a G-protein-coupled receptor.

scholarly journals A presynaptic endosomal trafficking pathway controls synaptic growth signaling

2011 ◽  
Vol 193 (1) ◽  
pp. 201-217 ◽  
Author(s):  
Avital A. Rodal ◽  
Aline D. Blunk ◽  
Yulia Akbergenova ◽  
Ramon A. Jorquera ◽  
Lauren K. Buhl ◽  
...  
Keyword(s):  
Endocytic Pathway ◽  
Physical Interaction ◽  
Endosomal Trafficking ◽  
Synaptic Growth ◽  
Recycling Endosomes ◽  
Sorting Nexin ◽  
Trafficking Pathway ◽  
Early Endosomes ◽  
Protein Receptors ◽  
Escrt Complex

Structural remodeling of synapses in response to growth signals leads to long-lasting alterations in neuronal function in many systems. Synaptic growth factor receptors alter their signaling properties during transit through the endocytic pathway, but the mechanisms controlling cargo traffic between endocytic compartments remain unclear. Nwk (Nervous Wreck) is a presynaptic F-BAR/SH3 protein that regulates synaptic growth signaling in Drosophila melanogaster. In this paper, we show that Nwk acts through a physical interaction with sorting nexin 16 (SNX16). SNX16 promotes synaptic growth signaling by activated bone morphogenic protein receptors, and live imaging in neurons reveals that SNX16-positive early endosomes undergo transient interactions with Nwk-containing recycling endosomes. We identify an alternative signal termination pathway in the absence of Snx16 that is controlled by endosomal sorting complex required for transport (ESCRT)–mediated internalization of receptors into the endosomal lumen. Our results define a presynaptic trafficking pathway mediated by SNX16, NWK, and the ESCRT complex that functions to control synaptic growth signaling at the interface between endosomal compartments.

scholarly journals Growth factor stimulation promotes multivesicular endosome biogenesis by prolonging recruitment of the late-acting ESCRT machinery

2019 ◽  
Vol 116 (14) ◽  
pp. 6858-6867 ◽  
Author(s):  
Kyle B. Quinney ◽  
Elisa B. Frankel ◽  
Raakhee Shankar ◽  
William Kasberg ◽  
Peter Luong ◽  
...  
Keyword(s):  
Growth Factor ◽  
Mammalian Cells ◽  
Light Sheet ◽  
Growth Conditions ◽  
Receptor Activation ◽  
Spatiotemporal Pattern ◽  
Growth Factor Signaling ◽  
Light Sheet Microscopy ◽  
Escrt Machinery ◽  
Escrt Complex

The formation of multivesicular endosomes (MVEs) mediates the turnover of numerous integral membrane proteins and has been implicated in the down-regulation of growth factor signaling, thereby exhibiting properties of a tumor suppressor. The endosomal sorting complex required for transport (ESCRT) machinery plays a key role in MVE biogenesis, enabling cargo selection and intralumenal vesicle (ILV) budding. However, the spatiotemporal pattern of endogenous ESCRT complex assembly and disassembly in mammalian cells remains poorly defined. By combining CRISPR/Cas9-mediated genome editing and live cell imaging using lattice light sheet microscopy (LLSM), we determined the native dynamics of both early- and late-acting ESCRT components at MVEs under multiple growth conditions. Specifically, our data indicate that ESCRT-0 accumulates quickly on endosomes, typically in less than 30 seconds, and its levels oscillate in a manner dependent on the downstream recruitment of ESCRT-I. Similarly, levels of the ESCRT-I complex also fluctuate on endosomes, but its average residency time is more than fivefold shorter compared with ESCRT-0. Vps4 accumulation is the most transient, however, suggesting that the completion of ILV formation occurs rapidly. Upon addition of epidermal growth factor (EGF), both ESCRT-I and Vps4 are retained at endosomes for dramatically extended periods of time, while ESCRT-0 dynamics are only modestly affected. Our findings are consistent with a model in which growth factor stimulation stabilizes late-acting components of the ESCRT machinery at endosomes to accelerate the rate of ILV biogenesis and attenuate signal transduction initiated by receptor activation.

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