Divergent Pathways in COS-7 Cells Mediate Defective Internalization and Intracellular Routing of Truncated G-CSFR Forms in SCN/AML

Hunter, Melissa; McLemore, Morgan L.; Link, Daniel C.; Loveland, Megan; Copelan, Alexander; Avalos, Belinda R.

doi:10.1371/journal.pone.0002452

Cited by 4 publications

(4 citation statements)

References 44 publications

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“…Inactivating the Stat5 signal is associated with receptor internalization and SOCS3 suppression (19,30). In our study, we observed a prolonged Stat5 activation in the G-CSFRIV + HSPCs.…”

Section: Discussionsupporting

confidence: 60%

miR-155 Is Associated with the Leukemogenic Potential of the Class IV Granulocyte Colony-Stimulating Factor Receptor in CD34+ Progenitor Cells

Zhang

Goudeva

Immenschuh

et al. 2014

Mol Med

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“…Inactivating the Stat5 signal is associated with receptor internalization and SOCS3 suppression (19,30). In our study, we observed a prolonged Stat5 activation in the G-CSFRIV + HSPCs.…”

Section: Discussionsupporting

confidence: 60%

miR-155 Is Associated with the Leukemogenic Potential of the Class IV Granulocyte Colony-Stimulating Factor Receptor in CD34+ Progenitor Cells

Zhang

Goudeva

Immenschuh

et al. 2014

Mol Med

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“…[D/E] XXX [L/I[L/I]] and [D/E]XXLL) seen in LIFR [ 132 ] and IL-2Rβ [ 133 ]), and the tyrosine-based motifs (i.e. YXXϕ), promoting clathrin-dependent endocytosis and internalization, first identified in the TPOR (YRRL) and later in the G-CSFR [ 134 , 135 ]. Additionally, phosphorylation dependent degrons (i.e.…”

Section: Resultsmentioning

confidence: 99%

Orchestration of signaling by structural disorder in class 1 cytokine receptors

et al. 2020

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Background: Class 1 cytokine receptors (C1CRs) are single-pass transmembrane proteins responsible for transmitting signals between the outside and the inside of cells. Remarkably, they orchestrate key biological processes such as proliferation, differentiation, immunity and growth through long disordered intracellular domains (ICDs), but without having intrinsic kinase activity. Despite these key roles, their characteristics remain rudimentarily understood. Methods: The current paper asks the question of why disorder has evolved to govern signaling of C1CRs by reviewing the literature in combination with new sequence and biophysical analyses of chain properties across the family. Results: We uncover that the C1CR-ICDs are fully disordered and brimming with SLiMs. Many of these short linear motifs (SLiMs) are overlapping, jointly signifying a complex regulation of interactions, including network rewiring by isoforms. The C1CR-ICDs have unique properties that distinguish them from most IDPs and we forward the perception that the C1CR-ICDs are far from simple strings with constitutively bound kinases. Rather, they carry both organizational and operational features left uncovered within their disorder, including mechanisms and complexities of regulatory functions. Conclusions: Critically, the understanding of the fascinating ability of these long, completely disordered chains to orchestrate complex cellular signaling pathways is still in its infancy, and we urge a perceptional shift away from the current simplistic view towards uncovering their full functionalities and potential.

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“…Some of these are frequent and are well- in LIFR [127] and IL-2Rb [128], and the tyrosine-based motifs (i.e. YXXf), promoting clathrindependent endocytosis and internalization, first identified in the TPOR (YRRL) and later in the G-CSFR [129,130]. Additionally, phosphorylation dependent degrons (i.e.…”

Section: Short Linear Motifs Allow Expansion Of the Interactomementioning

confidence: 99%

Orchestration of signaling by structural disorder in class 1 cytokine receptors

Seiffert

Bugge

Nygaard

et al. 2020

Preprint

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Background Class 1 cytokine receptors (C1CRs) are single-pass transmembrane proteins responsible for transmitting signals between the outside and the inside of cells. Remarkably, they orchestrate key biological processes such as proliferation, differentiation, immunity and growth through long disordered intracellular domains (ICDs), but without having intrinsic kinase activity. Despite these key roles, their characteristics remain rudimentarily understood. Methods The current paper asks the question of why disorder has evolved to govern signaling by the C1CRs by reviewing the literature in combination with new sequence and biophysical analyses of chain properties across the family. Results We uncover that the C1CR-ICDs are fully disordered and brimming with SLiMs. Many of these SLiMs are overlapping, jointly signifying a complex regulation of interactions, including network rewiring by isoforms. The C1CRs-ICDs have unique properties that distinguish them from most IDPs and we forward the perception that the C1CR-ICDs are far from simple strings with constitutively bound kinases. Rather, they carry both organizational and operational features left uncovered within their disorder, including mechanisms and complexities of regulatory functions. Conclusions Critically, the understanding of the fascinating ability of these long, completely disordered chains to orchestrate complex cellular signaling pathways is still in its infancy, and we urge a perceptional shift away from a simplistic view towards uncovering their full functionalities.

show abstract

Divergent Pathways in COS-7 Cells Mediate Defective Internalization and Intracellular Routing of Truncated G-CSFR Forms in SCN/AML

Cited by 4 publications

References 44 publications

miR-155 Is Associated with the Leukemogenic Potential of the Class IV Granulocyte Colony-Stimulating Factor Receptor in CD34+ Progenitor Cells

miR-155 Is Associated with the Leukemogenic Potential of the Class IV Granulocyte Colony-Stimulating Factor Receptor in CD34+ Progenitor Cells

Orchestration of signaling by structural disorder in class 1 cytokine receptors

Orchestration of signaling by structural disorder in class 1 cytokine receptors

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