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Article ; Online: Supply chain logistics - the role of the Golgi complex in extracellular matrix production and maintenance.

Hellicar, John / Stevenson, Nicola L / Stephens, David J / Lowe, Martin

2022 Volume 135, Issue 1

Abstract: The biomechanical and biochemical properties of connective tissues are determined by the composition and quality of their extracellular matrix. This, in turn, is highly dependent on the function and organisation of the secretory pathway. The Golgi ... ...

Abstract	The biomechanical and biochemical properties of connective tissues are determined by the composition and quality of their extracellular matrix. This, in turn, is highly dependent on the function and organisation of the secretory pathway. The Golgi complex plays a vital role in directing matrix output by co-ordinating the post-translational modification and proteolytic processing of matrix components prior to their secretion. These modifications have broad impacts on the secretion and subsequent assembly of matrix components, as well as their function in the extracellular environment. In this Review, we highlight the role of the Golgi in the formation of an adaptable, healthy matrix, with a focus on proteoglycan and procollagen secretion as example cargoes. We then discuss the impact of Golgi dysfunction on connective tissue in the context of human disease and ageing.
MeSH term(s)	Extracellular Matrix/metabolism ; Golgi Apparatus ; Humans ; Proteoglycans/genetics ; Proteoglycans/metabolism ; Secretory Pathway
Chemical Substances	Proteoglycans
Language	English
Publishing date	2022-01-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.258879
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Article ; Online: Cell biology: Collagen secretion explained.

Stephens, David J

Nature

2012 Volume 482, Issue 7386, Page(s) 474–475

MeSH term(s)	Animals ; COP-Coated Vesicles/chemistry ; COP-Coated Vesicles/metabolism ; Humans ; Ubiquitin/metabolism
Chemical Substances	Ubiquitin
Language	English
Publishing date	2012-02-22
Publishing country	England
Document type	News ; Comment
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/482474a
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Article ; Online: Functional coupling of microtubules to membranes - implications for membrane structure and dynamics.

Stephens, David J

Journal of cell science

2012 Volume 125, Issue Pt 12, Page(s) 2795–2804

Abstract: The microtubule network dictates much of the spatial patterning of the cytoplasm, and the coupling of microtubules to membranes controls the structure and positioning of organelles and directs membrane trafficking between them. The connection between ... ...

Abstract	The microtubule network dictates much of the spatial patterning of the cytoplasm, and the coupling of microtubules to membranes controls the structure and positioning of organelles and directs membrane trafficking between them. The connection between membranes and the microtubule cytoskeleton, and the way in which organelles are shaped and moved by interactions with the cytoskeleton, have been studied intensively in recent years. In particular, recent work has expanded our thinking of this topic to include the mechanisms by which membranes are shaped and how cargo is selected for trafficking as a result of coupling to the cytoskeleton. In this Commentary, I will discuss the molecular basis for membrane-motor coupling and the physiological outcomes of this coupling, including the way in which microtubule-based motors affect membrane structure, cargo sorting and vectorial trafficking between organelles. Whereas many core concepts of these processes are now well understood, key questions remain about how the coupling of motors to membranes is established and controlled, about the regulation of cargo and/or motor loading and about the control of directionality.
MeSH term(s)	Animals ; Humans ; Intracellular Membranes/chemistry ; Intracellular Membranes/metabolism ; Microtubules/chemistry ; Microtubules/metabolism ; Molecular Motor Proteins/metabolism ; Organelles/chemistry ; Organelles/metabolism ; Protein Transport
Chemical Substances	Molecular Motor Proteins
Language	English
Publishing date	2012-06-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.097675
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Article ; Online: Evaluation of treatment access and scope of a multistate hepatitis C virus Extension for Community Healthcare Outcomes telehealth service in the US Indian Health System, 2017‐2021

Wirth, Ashley N. / Cushman, Nicholas A. / Reilley, Brigg A. / Leston, Jessica D. / Mera, Jorge R. / Levander, Ximena A. / Stephens, David J.

The Journal of Rural Health. 2023 Mar., v. 39, no. 2 p.358-366

2023

Abstract: PURPOSE: American Indians/Alaska Native (AI/AN) persons are disproportionately affected by hepatitis C virus (HCV). The Northwest Portland Area Indian Health Board Indian Country Extension for Community Healthcare Outcomes (ECHO) telehealth clinic ... ...

Abstract	PURPOSE: American Indians/Alaska Native (AI/AN) persons are disproportionately affected by hepatitis C virus (HCV). The Northwest Portland Area Indian Health Board Indian Country Extension for Community Healthcare Outcomes (ECHO) telehealth clinic supports primary care providers (PCPs) in treating HCV. We evaluated the extent to which Indian Country ECHO increases access to HCV treatment and holistically serves AI/AN patients. METHODS: We conducted a retrospective descriptive analysis of Indian Country ECHO treatment recommendations from 2017 to 2021. Recommendations were classified into the following categories: HCV treatment with direct‐acting antiviral medication, prevention, substance use disorder treatment, lab or imaging orders, pharmacological considerations, behavior changes, other, and referral. Subanalysis of treatment recommendations was completed for patients with cirrhosis. FINDINGS: Of the 776 patients from 77 Indian Health System facilities who presented at Indian Country ECHO, 718 (93%) received treatment recommendations. Most patients (93%) received recommendations for HCV treatment by their PCP; only 3% received a recommendation for referral to a hepatologist or liver transplant center for additional care. Most patients received at least 1 recommendation beyond the scope of HCV treatment provision. Cirrhosis criteria were met by 8% of patients, of which 80% received recommendations for HCV treatment by their PCP and 25% received recommendations for referral to a specialist for additional care. CONCLUSIONS: Most patients presented at the Indian Country ECHO received recommendations for HCV treatment by their PCP, along with recommendations beyond the scope of HCV. Indian Country ECHO telehealth clinic provides comprehensive recommendations to effectively integrate evidence‐based HCV treatment with holistic care at the primary care level.
Keywords	Alaska Natives ; Hepatitis C virus ; drug therapy ; health services ; liver transplant ; rural health ; telemedicine
Language	English
Dates of publication	2023-03
Size	p. 358-366.
Publishing place	John Wiley & Sons, Ltd
Document type	Article ; Online
Note	JOURNAL ARTICLE
ZDB-ID	639160-6
ISSN	0890-765X
ISSN	0890-765X
DOI	10.1111/jrh.12733
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: ER-to-Golgi Transport: A Sizeable Problem.

McCaughey, Janine / Stephens, David J

Trends in cell biology

2019 Volume 29, Issue 12, Page(s) 940–953

Abstract: Metazoans require efficient and ordered secretion of extracellular matrix (ECM) to coordinate cell and tissue function. Many ECM proteins are atypically large and their demand during key stages of development presents a major challenge to the canonical ... ...

Abstract	Metazoans require efficient and ordered secretion of extracellular matrix (ECM) to coordinate cell and tissue function. Many ECM proteins are atypically large and their demand during key stages of development presents a major challenge to the canonical secretion machinery. While many of the molecular players in this pathway are known, little is understood about how they are integrated in time and space. Recent advances in gene engineering and super-resolution microscopy have underscored the spatiotemporal organisation of the endoplasmic reticulum (ER)-Golgi interface. These findings are challenging long-held models of vesicular transport of large matrix proteins, such as procollagen, and are implicating less well-defined carriers and direct interconnections between organelles. Here, we discuss current models describing the dynamics and mechanisms of ER-Golgi transport.
MeSH term(s)	Animals ; COP-Coated Vesicles/metabolism ; Endoplasmic Reticulum/metabolism ; Extracellular Matrix/metabolism ; Extracellular Matrix Proteins/metabolism ; Golgi Apparatus/metabolism ; Humans ; Protein Transport/physiology ; Vesicular Transport Proteins/metabolism
Chemical Substances	Extracellular Matrix Proteins ; Vesicular Transport Proteins
Language	English
Publishing date	2019-10-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	30122-x
ISSN	1879-3088 ; 0962-8924
ISSN (online)	1879-3088
ISSN	0962-8924
DOI	10.1016/j.tcb.2019.08.007
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Article ; Online: Roles for CEP170 in cilia function and dynein-2 assembly.

Weijman, Johannes F / Vuolo, Laura / Shak, Caroline / Pugnetti, Anna / Mukhopadhyay, Aakash G / Hodgson, Lorna R / Heesom, Kate J / Roberts, Anthony J / Stephens, David J

Journal of cell science

2024 Volume 137, Issue 8

Abstract: Primary cilia are essential eukaryotic organelles required for signalling and secretion. Dynein-2 is a microtubule-motor protein complex and is required for ciliogenesis via its role in facilitating retrograde intraflagellar transport (IFT) from the ... ...

Abstract	Primary cilia are essential eukaryotic organelles required for signalling and secretion. Dynein-2 is a microtubule-motor protein complex and is required for ciliogenesis via its role in facilitating retrograde intraflagellar transport (IFT) from the cilia tip to the cell body. Dynein-2 must be assembled and loaded onto IFT trains for entry into cilia for this process to occur, but how dynein-2 is assembled and how it is recycled back into a cilium remain poorly understood. Here, we identify centrosomal protein of 170 kDa (CEP170) as a dynein-2-interacting protein in mammalian cells. We show that loss of CEP170 perturbs intraflagellar transport and hedgehog signalling, and alters the stability of dynein-2 holoenzyme complex. Together, our data indicate a role for CEP170 in supporting cilia function and dynein-2 assembly.
MeSH term(s)	Cilia/metabolism ; Humans ; Microtubule-Associated Proteins/metabolism ; Microtubule-Associated Proteins/genetics ; Animals ; Dyneins/metabolism ; Dyneins/genetics ; Hedgehog Proteins/metabolism ; Hedgehog Proteins/genetics ; Signal Transduction ; Mice ; Flagella/metabolism
Chemical Substances	Microtubule-Associated Proteins ; Dyneins (EC 3.6.4.2) ; Hedgehog Proteins
Language	English
Publishing date	2024-05-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.261816
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Article ; Online: Structure and tethering mechanism of dynein-2 intermediate chains in intraflagellar transport.

Mukhopadhyay, Aakash G / Toropova, Katerina / Daly, Lydia / Wells, Jennifer N / Vuolo, Laura / Mladenov, Miroslav / Seda, Marian / Jenkins, Dagan / Stephens, David J / Roberts, Anthony J

The EMBO journal

2024 Volume 43, Issue 7, Page(s) 1257–1272

Abstract: Dynein-2 is a large multiprotein complex that powers retrograde intraflagellar transport (IFT) of cargoes within cilia/flagella, but the molecular mechanism underlying this function is still emerging. Distinctively, dynein-2 contains two identical force- ... ...

Abstract	Dynein-2 is a large multiprotein complex that powers retrograde intraflagellar transport (IFT) of cargoes within cilia/flagella, but the molecular mechanism underlying this function is still emerging. Distinctively, dynein-2 contains two identical force-generating heavy chains that interact with two different intermediate chains (WDR34 and WDR60). Here, we dissect regulation of dynein-2 function by WDR34 and WDR60 using an integrative approach including cryo-electron microscopy and CRISPR/Cas9-enabled cell biology. A 3.9 Å resolution structure shows how WDR34 and WDR60 use surprisingly different interactions to engage equivalent sites of the two heavy chains. We show that cilia can assemble in the absence of either WDR34 or WDR60 individually, but not both subunits. Dynein-2-dependent distribution of cargoes depends more strongly on WDR60, because the unique N-terminal extension of WDR60 facilitates dynein-2 targeting to cilia. Strikingly, this N-terminal extension can be transplanted onto WDR34 and retain function, suggesting it acts as a flexible tether to the IFT "trains" that assemble at the ciliary base. We discuss how use of unstructured tethers represents an emerging theme in IFT train interactions.
MeSH term(s)	Dyneins/metabolism ; Cryoelectron Microscopy ; Biological Transport ; Cilia/metabolism ; Flagella/metabolism
Chemical Substances	Dyneins (EC 3.6.4.2)
Language	English
Publishing date	2024-03-07
Publishing country	England
Document type	Journal Article
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.1038/s44318-024-00060-1
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Article ; Online: The warning stimulus as retrieval cue: The role of associative memory in temporal preparation.

Los, Sander A / Nieuwenstein, Jurre / Bouharab, Anass / Stephens, David J / Meeter, Martijn / Kruijne, Wouter

Cognitive psychology

2021 Volume 125, Page(s) 101378

Abstract: In a warned reaction time task, the warning stimulus (S1) initiates a process of temporal preparation, which promotes a speeded response to the impending target stimulus (S2). According to the multiple trace theory of temporal preparation (MTP), ... ...

Abstract	In a warned reaction time task, the warning stimulus (S1) initiates a process of temporal preparation, which promotes a speeded response to the impending target stimulus (S2). According to the multiple trace theory of temporal preparation (MTP), participants learn the timing of S2 by storing a memory trace on each trial, which contains a temporal profile of the events on that trial. On each new trial, S1 serves as a retrieval cue that implicitly and associatively activates memory traces created on earlier trials, which jointly drive temporal preparation for S2. The idea that S1 assumes this role as a retrieval cue was tested across eight experiments, in which two different S1s were associated with two different distributions of S1-S2 intervals: one with predominantly short and one with predominantly long intervals. Experiments differed regarding the S1 features that made up a pair, ranging from highly distinct (e.g., tone and flash) to more similar (e.g., red and green flash) and verbal (i.e., "short" vs "long"). Exclusively for pairs of highly distinct S1s, the results showed that the S1 cue modified temporal preparation, even in participants who showed no awareness of the contingency. This cueing effect persisted in a subsequent transfer phase, in which the contingency between S1 and the timing of S2 was broken - a fact participants were informed of in advance. Together, these findings support the role of S1 as an implicit retrieval cue, consistent with MTP.
MeSH term(s)	Cues ; Humans ; Learning ; Reaction Time
Language	English
Publishing date	2021-01-29
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1462875-2
ISSN	1095-5623 ; 0010-0285
ISSN (online)	1095-5623
ISSN	0010-0285
DOI	10.1016/j.cogpsych.2021.101378
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Article ; Online: COPII-dependent ER export in animal cells: adaptation and control for diverse cargo.

McCaughey, Janine / Stephens, David J

Histochemistry and cell biology

2018 Volume 150, Issue 2, Page(s) 119–131

Abstract: The export of newly synthesized proteins from the endoplasmic reticulum is fundamental to the ongoing maintenance of cell and tissue structure and function. After co-translational translocation into the ER, proteins destined for downstream intracellular ... ...

Abstract	The export of newly synthesized proteins from the endoplasmic reticulum is fundamental to the ongoing maintenance of cell and tissue structure and function. After co-translational translocation into the ER, proteins destined for downstream intracellular compartments or secretion from the cell are sorted and packaged into transport vesicles by the COPII coat protein complex. The fundamental discovery and characterization of the pathway has now been augmented by a greater understanding of the role of COPII in diverse aspects of cell function. We now have a deep understanding of how COPII contributes to the trafficking of diverse cargoes including extracellular matrix molecules, developmental signalling proteins, and key metabolic factors such as lipoproteins. Structural and functional studies have shown that the COPII coat is both highly flexible and subject to multiple modes of regulation. This has led to new discoveries defining roles of COPII in development, autophagy, and tissue organization. Many of these newly emerging features of the canonical COPII pathway are placed in a context of procollagen secretion because of the fundamental interest in how a coat complex that typically generates 80-nm transport vesicles can package a cargo reported to be over 300 nm. Here we review the current understanding of COPII and assess the current consensus on its role in packaging diverse cargo proteins.
MeSH term(s)	Animals ; COP-Coated Vesicles/metabolism ; Endoplasmic Reticulum/metabolism ; Protein Transport ; Proteins/metabolism
Chemical Substances	Proteins
Language	English
Publishing date	2018-06-18
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	1222930-1
ISSN	1432-119X ; 0301-5564 ; 0948-6143
ISSN (online)	1432-119X
ISSN	0301-5564 ; 0948-6143
DOI	10.1007/s00418-018-1689-2
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Book: Methods for analysis of Golgi complex function

Perez, Franck / Stephens, David J

(Methods in cell biology, ; volume 118)

2013

Author's details	edited by Franck Perez, David J. Stephens
Series title	Methods in cell biology, ; volume 118
MeSH term(s)	Golgi Apparatus/physiology ; Microscopy/methods ; Image Processing, Computer-Assisted/methods
Language	English
Size	xx, 443 pages, [34] pages of plates :, illustrations (some color) ;, 24 cm.
Edition	First edition.
Document type	Book
ISBN	9780124171640 ; 0124171648
Database	Catalogue of the US National Library of Medicine (NLM)

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