Peroxiredoxin-controlled G-CSF signalling at the endoplasmic reticulum–early endosome interface

Palande, Karishma; Roovers, Onno; Gits, Judith; Verwijmeren, Carola; Iuchi, Yoshihito; Fujii, Junichi; Neel, Benjamin G.; Karisch, Robert; Tavernier, Jan; Touw, Ivo P.

doi:10.1242/jcs.089656

Cited by 50 publications

(43 citation statements)

References 56 publications

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“…Other examples, which are connected to H 2 O 2 transit across the ER membrane, are granulocyte colonystimulating factor receptor signaling [29], oxidative DNA damage in response to cellular stresses [30][31][32], activation of survival pathways upon H 2 O 2 generation in the ER [33,34], and the regulatory roles of ER-luminal peroxidases in various settings of cytosolic signal transduction [29,[35][36][37][38]. These findings clearly indicate the permeability of the ER membrane for H 2 O 2 .…”

Section: H 2 O 2 Can Readily Permeate Through the Endoplasmic Reticulmentioning

confidence: 98%

Transit of H2O2 across the endoplasmic reticulum membrane is not sluggish

Appenzeller-Herzog¹,

Bánhegyi

Bogeski

et al. 2016

Free Radical Biology and Medicine

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Section: H 2 O 2 Can Readily Permeate Through the Endoplasmic Reticulmentioning

confidence: 98%

Transit of H2O2 across the endoplasmic reticulum membrane is not sluggish

Appenzeller-Herzog¹,

Bánhegyi

Bogeski

et al. 2016

Free Radical Biology and Medicine

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“…Oxysterol-binding protein-related protein 5 (ORP5), an ERresident transmembrane protein related to ORP1L, contacts the late endosomal cholesterol transporter Niemann-Pick type C1 (NPC1) (Du et al, 2011) and hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs, also known as HGS) that is located on endosomes (Pridgeon et al, 2009;Du et al, 2012). Furthermore, the ER protein-tyrosine phosphatase 1B (PTP1B) interacts with epidermal growth factor receptor (EGFR) as well as with the granulocyte colony-stimulating factor receptor (G-CSFR, also known as CSF3R) -the later involving Prdx4 (Eden et al, 2010;Palande et al, 2011). Apart from the interaction between PTP1B and EGFR or G-CSFR, the abovementioned interactions (ORP1L-or MLN64 and VAP-A, and ORP5 and NPC1) all involve cholesterol.…”

Section: Protein Pairs At the Er-endosome Interfacementioning

confidence: 99%

“…EGFR is subsequently internalized, and it maintains its signaling competence until it is dephosphorylated by the ER tyrosine-phosphatase PTP1B and/or sequestered within multivesicular bodies (Eden et al, 2010). In an analogous process, activated G-CSFR is dephosphorylated by PTP1B to downregulate its signaling (Palande et al, 2011). Dephosphorylation of tyrosine-phosphorylated transmembrane receptor proteins by PTP1B at ER-late-endosomes MCSs is probably not limited to EGFR and G-CSFR, as PTP1B has several other known substrates (Yip et al, 2010), including subunits of the ESCRT complex (Hrs and STAM subunits) that are involved in ILV formation (Stuible et al, 2010;Eden et al, 2012).…”

Section: Er In Control Of Endosomal Maturationmentioning

confidence: 99%

Small regulators, major consequences – Ca2+ and cholesterol at the endosome–ER interface

Kant

Neefjes

2014

Journal of Cell Science

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The ER is the largest cellular compartment and a major storage site for lipids and ions. In recent years, much attention has focused on contacts between the ER and other organelles, and one particularly intimate relationship is that between the ER and the endosomal system. ER-endosome contacts intensify when endosomes mature, and the ER participates in endosomal processes, such as the termination of surface receptor signaling, multi-vesicular body formation, and transport and fusion events. Cholesterol and Ca 2+ are transferred between the ER and endosomes, possibly acting as messengers for ER-endosome crosstalk. Here, we summarize different types of ER-endosomal communication and discuss membrane contact sites that might facilitate this crosstalk. We review the protein pairs that interact at the ER-endosome interface and find that many of these have a role in cholesterol exchange. We also summarize Ca 2+ exchange between the ER and endosomes, and hypothesize that ERendosome contacts integrate several cellular functions to guide endosomal maturation. We post the hypothesis that failure in ERendosome contacts is an unrecognized but important contributor to diseases, such as Niemann-Pick type C disease, Alzheimer's disease and amyotrophic lateral sclerosis.

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“…19 Colony assays of these transduced progenitors were performed as described previously. 20 Further details of these procedures are provided in supplemental Methods. …”

mentioning

confidence: 99%

Sequential gain of mutations in severe congenital neutropenia progressing to acute myeloid leukemia

Beekman

Valkhof

Sanders

et al. 2012

Blood

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156

178

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Severe congenital neutropenia (SCN) is a BM failure syndrome with a high risk of progression to acute myeloid leukemia (AML). The underlying genetic changes involved in SCN evolution to AML are largely unknown. We obtained serial hematopoietic samples from an SCN patient who developed AML 17 years after the initiation of G-CSF treatment. Nextgeneration sequencing was performed to identify mutations during disease progression. In the AML phase, we found 12 acquired nonsynonymous mutations. Three of these, in CSF3R, LLGL2, and ZC3H18, co-occurred in a subpopulation of progenitor cells already in the early SCN phase. This population expanded over time, whereas clones harboring only CSF3R mutations disappeared from the BM. The other 9 mutations were only apparent in the AML cells and affected known AML-associated genes (RUNX1 and ASXL1) and chromatin remodelers (SUZ12 and EP300). In addition, a novel CSF3R mutation that conferred autonomous proliferation to myeloid progenitors was found. We conclude that progression from SCN to AML is a multistep process, with distinct mutations arising early during the SCN phase and others later in AML development. IntroductionSevere congenital neutropenia (SCN) is a BM failure syndrome characterized by strongly reduced neutrophil counts and recurrent, potentially life-threatening, opportunistic bacterial infections. Treatment with G-CSF elevates peripheral neutrophil counts and reduces the risk of infections. 1 Leukemic progression of SCN is a major concern, with an estimated overall cumulative incidence of approximately 20% after 15 years of G-CSF treatment. 2 Constitutional mutations in the gene encoding neutrophil elastase (ELANE) are common defects in SCN. 3 In addition, the acquisition of nonsense mutations in the gene encoding the G-CSF receptor (CSF3R) is a unique feature in SCN patients. [4][5][6][7] These mutations lead to the expression of truncated CSF3R proteins, also known as the ␦ forms. In cell-line models, truncated CSF3R proteins are hampered in transducing the signals required for proper neutrophil differentiation, confer increased proliferative responses to G-CSF treatment, but do not cause leukemia in mice. [4][5][6][8][9][10][11] CSF3R␦ mutations can be detected in approximately 30% of SCN patients. In some cases, distinct clones with different CSF3R␦ mutations are present for many years. 7,12 After evolution of SCN toward acute myeloid leukemia (AML), CSF3R␦ mutations are found in approximately 80% of patients. 12 Until now, all reported SCN/AML patients harboring a CSF3R␦ mutation in the SCN phase also carry this mutation in the leukemic phase. These observations suggest that leukemic progression in SCN follows a unique pattern, with CSF3R␦ mutations as an early event, followed by additional genetic and epigenetic events that are essential for full leukemic transformation. Chromosomal aberrations such as loss of chromosome 7 and gain of chromosome 21 are apparent in AML arising from SCN and other BM failure syndromes such as Fanconi anemia and Shwachman-Dia...

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Peroxiredoxin-controlled G-CSF signalling at the endoplasmic reticulum–early endosome interface

Cited by 50 publications

References 56 publications

Transit of H2O2 across the endoplasmic reticulum membrane is not sluggish

Transit of H2O2 across the endoplasmic reticulum membrane is not sluggish

Small regulators, major consequences – Ca2+ and cholesterol at the endosome–ER interface

Sequential gain of mutations in severe congenital neutropenia progressing to acute myeloid leukemia

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