Connecting the Cytoskeleton to the Endoplasmic Reticulum and Golgi

Gurel, Pinar S.; Hatch, Anna L.; Higgs, Henry N.

doi:10.1016/j.cub.2014.05.033

Cited by 153 publications

(144 citation statements)

References 161 publications

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“…In conclusion, we describe Gp96 as novel regulator of PM blebbing during PFT-induced PM damage and infection and further highlight the important crosstalk between the ER and cytoskeleton which impacts fundamental cellular processes [47] and innate responses to bacteria.…”

Section: Embo Reportsmentioning

confidence: 99%

Endoplasmic reticulum chaperone Gp96 controls actomyosin dynamics and protects against pore‐forming toxins

et al. 2016

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During infection, plasma membrane (PM) blebs protect host cells against bacterial pore-forming toxins (PFTs), but were also proposed to promote pathogen dissemination. However, the details and impact of blebbing regulation during infection remained unclear. Here, we identify the endoplasmic reticulum chaperone Gp96 as a novel regulator of PFT-induced blebbing. Gp96 interacts with non-muscle myosin heavy chain IIA (NMHCIIA) and controls its activity and remodelling, which is required for appropriate coordination of bleb formation and retraction. This mechanism involves NMHCIIA-Gp96 interaction and their recruitment to PM blebs and strongly resembles retraction of uropod-like structures from polarized migrating cells, a process that also promotes NMHCIIA-Gp96 association. Consistently, Gp96 and NMHCIIA not only protect the PM integrity from listeriolysin O (LLO) during infection by Listeria monocytogenes but also affect cytoskeletal organization and cell migration. Finally, we validate the association between Gp96 and NMHCIIA in vivo and show that Gp96 is required to protect hosts from LLO-dependent killing.

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Section: Embo Reportsmentioning

confidence: 99%

Endoplasmic reticulum chaperone Gp96 controls actomyosin dynamics and protects against pore‐forming toxins

et al. 2016

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“…Given the role of the basal body and microtubules in regulating trafficking through the secretory pathway, we also examined the structure of these compartments in the affected cells [27]. As judged by immunofluorescence, there was no change in the morphology of the endoplasmic reticulum and the cis - and trans -Golgi of UDP-3331 compared to control adult dermal fibroblasts (Fig.…”

Section: Resultsmentioning

confidence: 99%

Abnormal glycosylation in Joubert syndrome type 10

Kane

Davids

Bond

et al. 2017

Cilia

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BackgroundThe discovery of disease pathogenesis requires systematic agnostic screening of multiple homeostatic processes that may become deregulated. We illustrate this principle in the evaluation and diagnosis of a 5-year-old boy with Joubert syndrome type 10 (JBTS10). He carried the OFD1 mutation p.Gln886Lysfs*2 (NM_003611.2: c.2656del) and manifested features of Joubert syndrome.MethodsWe integrated exome sequencing, MALDI-TOF mass spectrometry analyses of plasma and cultured dermal fibroblasts glycomes, and full clinical evaluation of the proband. Analyses of cilia formation and lectin staining were performed by immunofluorescence. Measurement of cellular nucleotide sugar levels was performed with high-performance anion-exchange chromatography with pulsed amperometric detection. Statistical analyses utilized the Student’s and Fisher’s exact t tests.ResultsGlycome analyses of plasma and cultured dermal fibroblasts identified abnormal N- and O-linked glycosylation profiles. These findings replicated in two unrelated males with OFD1 mutations. Cultured fibroblasts from affected individuals had a defect in ciliogenesis. The proband’s fibroblasts also had an abnormally elevated nuclear sialylation signature and increased total cellular levels of CMP-sialic acid. Ciliogenesis and each glycosylation anomaly were rescued by expression of wild-type OFD1.ConclusionsThe rescue of ciliogenesis and glycosylation upon reintroduction of WT OFD1 suggests that both contribute to the pathogenesis of JBTS10.Electronic supplementary materialThe online version of this article (doi:10.1186/s13630-017-0048-6) contains supplementary material, which is available to authorized users.

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“…In addition to the formation of lateral contacts between the microtubule lattice and membrane-enclosed compartments, microtubule plus-ends and membranes can also form dynamic connections that can reshape or position a wide variety of intracellular structures 56 . In Xenopus egg extracts, growing microtubule plus-ends can interact with membranes and push out long, extended endoplasmic reticulum (ER-)tubes 149,151 .…”

Section: Pushing Forces Generated By Microtubule Polymerizationmentioning

confidence: 99%

Understanding force-generating microtubule systems through in vitro reconstitution

Vleugel

Kok

Dogterom

2016

Cell Adhesion & Migration

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Microtubules switch between growing and shrinking states, a feature known as dynamic instability. The biochemical parameters underlying dynamic instability are modulated by a wide variety of microtubule-associated proteins that enable the strict control of microtubule dynamics in cells. The forces generated by controlled growth and shrinkage of microtubules drive a large range of processes, including organelle positioning, mitotic spindle assembly, and chromosome segregation. In the past decade, our understanding of microtubule dynamics and microtubule force generation has progressed significantly. Here, we review the microtubule-intrinsic process of dynamic instability, the effect of external factors on this process, and how the resulting forces act on various biological systems. Recently, reconstitution-based approaches have strongly benefited from extensive biochemical and biophysical characterization of individual components that are involved in regulating or transmitting microtubule-driven forces. We will focus on the current state of reconstituting increasingly complex biological systems and provide new directions for future developments.

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Connecting the Cytoskeleton to the Endoplasmic Reticulum and Golgi

Cited by 153 publications

References 161 publications

Endoplasmic reticulum chaperone Gp96 controls actomyosin dynamics and protects against pore‐forming toxins

Endoplasmic reticulum chaperone Gp96 controls actomyosin dynamics and protects against pore‐forming toxins

Abnormal glycosylation in Joubert syndrome type 10

Understanding force-generating microtubule systems through in vitro reconstitution

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