The Biogenesis of Lysosomes and Lysosome-Related Organelles

Luzio, J. Paul; Hackmann, Yvonne; Dieckmann, Nele M. G.; Griffiths, Gillian M.

doi:10.1101/cshperspect.a016840

Cited by 270 publications

(264 citation statements)

References 130 publications

Supporting

Mentioning

260

Contrasting

Unclassified

Order By: Relevance

“…5). It is well-established that, in specialized cells, Rab32, in conjunction with other Rab GTPases and multiprotein assemblies known as BLOC 1, 2, and 3, coordinates the delivery of specific cargo to lysosome-related compartments such as melanosomes and T-cell granules (55)(56)(57)(58). This cargo includes antimicrobial compounds as well as enzymes required for the synthesis of melanin and its phenyl oxidase intermediates, many of which have potent antimicrobial activity (56,(58)(59)(60)(61).…”

Section: Typhoid Toxin and S Typhi Host Specificitymentioning

confidence: 99%

Typhoid toxin provides a window into typhoid fever and the biology ofSalmonellaTyphi

Galán

2016

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Salmonella Typhi is the cause of typhoid fever, a disease that has challenged humans throughout history and continues to be a major public health concern. Unlike infections with most other Salmonellae, which result in self-limiting gastroenteritis, typhoid fever is a life-threatening systemic disease. Furthermore, in contrast to most Salmonellae, which can infect a broad range of hosts, S. Typhi is a strict human pathogen. The unique features of S. Typhi pathogenesis and its stringent host specificity have been a long-standing puzzle. The discovery of typhoid toxin not only has provided major insight into these questions but also has offered unique opportunities to develop novel therapeutic and prevention strategies to combat typhoid fever.

show abstract

Section: Typhoid Toxin and S Typhi Host Specificitymentioning

confidence: 99%

Typhoid toxin provides a window into typhoid fever and the biology ofSalmonellaTyphi

Galán

2016

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…They cover the molecular machineries responsible for the compartmental organization and function of endosomes (WandingerNess and Zerial 2014) and sorting and transport along endolysosomal pathways (Bissig and Gruenberg 2013;Henne et al 2013;Burd and Cullen 2014;Piper et al 2014). Lysosomes and lysosome-related organelles are discussed in the article by Luzio et al 2014). Once thought to be "dead-end" receptacles responsible only for degradation, lysosomes have revealed themselves as dynamic and functionally diverse organelles that can fuse with the plasma membrane in response to extracellular cues.…”

Section: Overview Of Articlesmentioning

confidence: 99%

Endocytosis: Past, Present, and Future

Schmid

Sorkin

Zerial

2014

Cold Spring Harbor Perspectives in Biology

View full text Add to dashboard Cite

“…The protein machinery that controls the fusion of late endosome and lysosomal compartments with the plasma membrane is now relatively well documented and involves syntaxin 7 (STX7), STX8, vesicle-associated membrane protein 7 (VAMP7) and VAMP8, which are all members of the SNARE protein family (Kent et al, 2012;Luzio et al, 2010;Luzio et al, 2014;Pryor et al, 2004). Chavrier and co-workers have established that VAMP7 and the exocyst complex deliver a late endosomal pool of membrane type 1 metalloproteinase (MT1-MMP, also known as MMP14) to the cell surface for ECM proteolysis, which is crucial for invasive migration (Steffen et al, 2008).…”

Section: Snare Proteins On Endomembranes Interact With Cholesterolmentioning

confidence: 99%

Role of cholesterol in SNARE-mediated trafficking on intracellular membranes

Enrich

Rentero

Hierro

et al. 2015

Journal of Cell Science

View full text Add to dashboard Cite

The cell surface delivery of extracellular matrix (ECM) and integrins is fundamental for cell migration in wound healing and during cancer cell metastasis. This process is not only driven by several soluble NSF attachment protein (SNAP) receptor (SNARE) proteins, which are key players in vesicle transport at the cell surface and intracellular compartments, but is also tightly modulated by cholesterol. Cholesterol-sensitive SNAREs at the cell surface are relatively well characterized, but it is less well understood how altered cholesterol levels in intracellular compartments impact on SNARE localization and function. Recent insights from structural biology, protein chemistry and cell microscopy have suggested that a subset of the SNAREs engaged in exocytic and retrograde pathways dynamically 'sense' cholesterol levels in the Golgi and endosomal membranes. Hence, the transport routes that modulate cellular cholesterol distribution appear to trigger not only a change in the location and functioning of SNAREs at the cell surface but also in endomembranes. In this Commentary, we will discuss how disrupted cholesterol transport through the Golgi and endosomal compartments ultimately controls SNARE-mediated delivery of ECM and integrins to the cell surface and, consequently, cell migration.

show abstract

The Biogenesis of Lysosomes and Lysosome-Related Organelles

Cited by 270 publications

References 130 publications

Typhoid toxin provides a window into typhoid fever and the biology ofSalmonellaTyphi

Typhoid toxin provides a window into typhoid fever and the biology ofSalmonellaTyphi

Endocytosis: Past, Present, and Future

Role of cholesterol in SNARE-mediated trafficking on intracellular membranes

Contact Info

Product

Resources

About