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Article ; Online: Axonal transport of late endosomes and amphisomes is selectively modulated by local Ca

Lie, Pearl P Y / Yoo, Lang / Goulbourne, Chris N / Berg, Martin J / Stavrides, Philip / Huo, Chunfeng / Lee, Ju-Hyun / Nixon, Ralph A

Science advances

2022 Volume 8, Issue 17, Page(s) eabj5716

Abstract: Dysfunction and mistrafficking of organelles in autophagy- and endosomal-lysosomal pathways are implicated in neurodegenerative diseases. Here, we reveal selective vulnerability of maturing degradative organelles (late endosomes/amphisomes) to disease- ... ...

Abstract	Dysfunction and mistrafficking of organelles in autophagy- and endosomal-lysosomal pathways are implicated in neurodegenerative diseases. Here, we reveal selective vulnerability of maturing degradative organelles (late endosomes/amphisomes) to disease-relevant local calcium dysregulation. These organelles undergo exclusive retrograde transport in axons, with occasional pauses triggered by regulated calcium efflux from agonist-evoked transient receptor potential cation channel mucolipin subfamily member 1 (TRPML1) channels-an effect greatly exaggerated by exogenous agonist mucolipin synthetic agonist 1 (ML-SA1). Deacidification of degradative organelles, as seen after Presenilin 1 (PSEN1) loss of function, induced pathological constitutive "inside-out" TRPML1 hyperactivation, slowing their transport comparably to ML-SA1 and causing accumulation in dystrophic axons. The mechanism involved calcium-mediated c-Jun N-terminal kinase (JNK) activation, which hyperphosphorylated dynein intermediate chain (DIC), reducing dynein activity. Blocking TRPML1 activation, JNK activity, or DIC1B serine-80 phosphorylation reversed transport deficits in
Language	English
Publishing date	2022-04-29
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.abj5716
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Article ; Online: Lysosome trafficking and signaling in health and neurodegenerative diseases.

Lie, Pearl P Y / Nixon, Ralph A

Neurobiology of disease

2018 Volume 122, Page(s) 94–105

Abstract: Lysosomes, single-membrane organelles defined by a uniquely strong acidic lumenal pH and high content of acid hydrolases, are the shared degradative compartments of the endocytic and autophagic pathways. These pathways, and especially lysosomes, are ... ...

Abstract	Lysosomes, single-membrane organelles defined by a uniquely strong acidic lumenal pH and high content of acid hydrolases, are the shared degradative compartments of the endocytic and autophagic pathways. These pathways, and especially lysosomes, are points of particular vulnerability in many neurodegenerative diseases. Beyond the role of lysosomes in substrate degradation, new findings have ascribed to lysosomes the leading role in sensing and responding to cellular nutrients, growth factors and cellular stress. This review aims to integrate recent concepts of basic lysosome biology and pathobiology as a basis for understanding neurodegenerative disease pathogenesis. Here, we discuss the newly recognized signaling functions of lysosomes and specific aspects of lysosome biology in neurons while re-visiting the classical defining criteria for lysosomes and the importance of preserving strict definitions. Our discussion emphasizes dynein-mediated axonal transport of maturing degradative organelles, with further consideration of their roles in synaptic function. We finally examine how distinctive underlying disturbances of lysosomes in various neurodegenerative diseases result in unique patterns of auto/endolysosomal mistrafficking. The rapidly emerging understanding of lysosomal trafficking and disruptions in lysosome signaling is providing valuable clues to new targets for disease-modifying therapies.
MeSH term(s)	Animals ; Humans ; Lysosomes/metabolism ; Neurodegenerative Diseases/metabolism ; Neurons/metabolism
Language	English
Publishing date	2018-05-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1211786-9
ISSN	1095-953X ; 0969-9961
ISSN (online)	1095-953X
ISSN	0969-9961
DOI	10.1016/j.nbd.2018.05.015
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Zs.A 4444: Show issues

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Article ; Online: Post-Golgi carriers, not lysosomes, confer lysosomal properties to pre-degradative organelles in normal and dystrophic axons.

Lie, Pearl P Y / Yang, Dun-Sheng / Stavrides, Philip / Goulbourne, Chris N / Zheng, Ping / Mohan, Panaiyur S / Cataldo, Anne M / Nixon, Ralph A

Cell reports

2021 Volume 35, Issue 4, Page(s) 109034

Abstract: Lysosomal trafficking and maturation in neurons remain poorly understood and are unstudied in vivo despite high disease relevance. We generated neuron-specific transgenic mice to track vesicular CTSD acquisition, acidification, and traffic within the ... ...

Abstract	Lysosomal trafficking and maturation in neurons remain poorly understood and are unstudied in vivo despite high disease relevance. We generated neuron-specific transgenic mice to track vesicular CTSD acquisition, acidification, and traffic within the autophagic-lysosomal pathway in vivo, revealing that mature lysosomes are restricted from axons. Moreover, TGN-derived transport carriers (TCs), not lysosomes, supply lysosomal components to axonal organelles. Ultrastructurally distinctive TCs containing TGN and lysosomal markers enter axons, engaging autophagic vacuoles and late endosomes. This process is markedly upregulated in dystrophic axons of Alzheimer models. In cultured neurons, most axonal LAMP1 vesicles are weakly acidic TCs that shuttle lysosomal components bidirectionally, conferring limited degradative capability to retrograde organelles before they mature fully to lysosomes within perikarya. The minor LAMP1 subpopulation attaining robust acidification are retrograde Rab7
MeSH term(s)	Animals ; Axons/metabolism ; Disease Models, Animal ; Golgi Apparatus/metabolism ; Mice ; Mice, Transgenic ; Organelles/metabolism
Language	English
Publishing date	2021-04-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2021.109034
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Article ; Online: Signalling pathways regulating the blood-testis barrier.

Lie, Pearl P Y / Cheng, C Yan / Mruk, Dolores D

The international journal of biochemistry & cell biology

2012 Volume 45, Issue 3, Page(s) 621–625

Abstract: Throughout mammalian spermatogenesis, preleptotene/leptotene spermatocytes traverse the blood-testis barrier during stages VIII-XI of the seminiferous epithelial cycle while trapped within a dynamic intermediate compartment that is sealed at north and ... ...

Abstract	Throughout mammalian spermatogenesis, preleptotene/leptotene spermatocytes traverse the blood-testis barrier during stages VIII-XI of the seminiferous epithelial cycle while trapped within a dynamic intermediate compartment that is sealed at north and south poles by tight junctions, basal ectoplasmic specializations, desmosomes and gap junctions. In order for spermatocytes to gain entry into the adluminal compartment of the seminiferous epithelium for continued development, 'old' junctions present above migrating spermatocytes disassemble, while 'new' junctions assemble simultaneously below these germ cells. In this way, the integrity of the blood-testis barrier and the homeostasis of the seminiferous epithelium can remain intact during spermatogenesis. Previous studies have shown an array of cellular events, including protein internalization and cytoskeletal remodeling, to underline blood-testis barrier restructuring, whereas other studies have reported BTB dysfunction to associate with activation of the p38 mitogen-activated protein kinase pathway. Herein, we discuss the signaling pathways and mechanisms involved in blood-testis barrier restructuring in the mammalian testis.
MeSH term(s)	Animals ; Autocrine Communication ; Blood-Testis Barrier/metabolism ; Blood-Testis Barrier/physiology ; Humans ; Male ; Paracrine Communication ; Sertoli Cells/cytology ; Sertoli Cells/metabolism ; Signal Transduction ; Testis/physiology ; Testosterone/metabolism ; Testosterone/physiology ; p38 Mitogen-Activated Protein Kinases/metabolism
Chemical Substances	Testosterone (3XMK78S47O) ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24)
Language	English
Publishing date	2012-12-20
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1228429-4
ISSN	1878-5875 ; 1357-2725
ISSN (online)	1878-5875
ISSN	1357-2725
DOI	10.1016/j.biocel.2012.12.009
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Zs.A 431: Show issues

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Article ; Online: The biology of interleukin-1: emerging concepts in the regulation of the actin cytoskeleton and cell junction dynamics.

Lie, Pearl P Y / Cheng, C Yan / Mruk, Dolores D

Cellular and molecular life sciences : CMLS

2011 Volume 69, Issue 4, Page(s) 487–500

Abstract: Interleukin (IL)-1 is a proinflammatory cytokine with important roles in innate immunity, as well as in normal tissue homeostasis. Interestingly, recent studies have also shown IL-1 to function in the dynamics of the actin cytoskeleton and cell junctions. ...

Abstract	Interleukin (IL)-1 is a proinflammatory cytokine with important roles in innate immunity, as well as in normal tissue homeostasis. Interestingly, recent studies have also shown IL-1 to function in the dynamics of the actin cytoskeleton and cell junctions. For example, treatment of different epithelia with IL-1α often results in the restructuring of the actin network and cell junctions, thereby leading to junction disassembly. In this review, we highlight new and interesting findings that show IL-1 to be a critical player of restructuring events in the seminiferous epithelium of the testis during spermatogenesis.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Humans ; Intercellular Junctions/metabolism ; Interleukin-1/metabolism ; Interleukin-1/physiology ; NF-kappa B/metabolism ; Signal Transduction ; Spermatogenesis ; rho GTP-Binding Proteins/metabolism
Chemical Substances	Interleukin-1 ; NF-kappa B ; rho GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2011-07-09
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-011-0760-0
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Zs.A 195: Show issues

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Article ; Online: Interleukin-1alpha is a regulator of the blood-testis barrier.

Lie, Pearl P Y / Cheng, C Yan / Mruk, Dolores D

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2010 Volume 25, Issue 4, Page(s) 1244–1253

Abstract: Throughout spermatogenesis, the Sertoli cell blood-testis barrier (BTB) is strictly regulated by cytokines, which mediate its timely restructuring, thereby allowing spermatocytes to enter the adluminal compartment of the seminiferous epithelium for ... ...

Abstract	Throughout spermatogenesis, the Sertoli cell blood-testis barrier (BTB) is strictly regulated by cytokines, which mediate its timely restructuring, thereby allowing spermatocytes to enter the adluminal compartment of the seminiferous epithelium for development into spermatozoa. The aim herein was to investigate whether germ cells play a role in BTB restructuring via the action of interleukin-1α (IL-1α) since germ cells are known to control Sertoli cell production of this cytokine, and if yes, how these effects are mediated. When Sertoli cells were isolated from Sprague-Dawley rats and plated at high density, IL-1α (100 pg/ml) was shown to "open" the Sertoli cell barrier when its integrity was assessed by transepithelial electrical resistance measurements. Further investigation of Sertoli cells treated with IL-1α revealed striking changes in the cellular distribution of actin filaments when compared to untreated cells. These effects at the Sertoli cell barrier were mediated, in part, by epidermal growth factor receptor pathway substrate 8 (Eps8; an actin bundling and barbed-end capping protein) and actin-related protein 3 (Arp3; a component of the actin nucleation machinery). As important, an increase in the kinetics of occludin internalization but a decrease in its rate of degradation was noted following IL-1α treatment. These results indicate that IL-1α is a critical regulator of BTB dynamics.
MeSH term(s)	Actin Cytoskeleton/drug effects ; Animals ; Blood-Testis Barrier/drug effects ; Cells, Cultured ; Endocytosis/drug effects ; Interleukin-1alpha/pharmacology ; Interleukin-1alpha/physiology ; Male ; Membrane Proteins/metabolism ; Occludin ; Phosphoproteins/metabolism ; Rats ; Rats, Sprague-Dawley ; Sertoli Cells/drug effects ; Spermatogenesis/drug effects ; Tight Junctions/drug effects ; Zonula Occludens-1 Protein
Chemical Substances	Interleukin-1alpha ; Membrane Proteins ; Occludin ; Ocln protein, rat ; Phosphoproteins ; Tjp1 protein, rat ; Zonula Occludens-1 Protein
Language	English
Publishing date	2010-12-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.10-169995
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Zs.A 2266: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 296: Show issues

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Article: Focal adhesion kinase and actin regulatory/binding proteins that modulate F-actin organization at the tissue barrier: Lesson from the testis.

Cheng, C Yan / Lie, Pearl P Y / Wong, Elissa W P / Mruk, Dolores D

Tissue barriers

2014 Volume 1, Issue 2, Page(s) e24252

Abstract: ... fibroblasts and also tumor cells. In the testis, however, FAK and two of its phosphorylated forms, p-FAK-Tyr ... and spatiotemporal expression of p-FAK-Tyr(407) and -Tyr(397) are crucial to the regulation ... cycle. A recent report (Lie et al. PNAS 109:12562-12567, 2012) has demonstrated that the stage-specific ...

Abstract	Focal adhesion kinase (FAK), as its name implied, is an important mediator of integrin-based signaling function in mammalian cells at the focal adhesion complex (FAC, also known as focal contact) at the cell-extracellular matrix interface. FAK is intimately related to cell movement, such as in macrophages, fibroblasts and also tumor cells. In the testis, however, FAK and two of its phosphorylated forms, p-FAK-Tyr(407) and -Tyr(397), are not found at the FAC since there is no ultrastructure analogous or similar to FAC in the mammalian testis vs. other epithelia. Instead, FAK and its two phosphorylated forms are detected along the seminiferous epithelium in the rat testis at the cell-cell interface in a testis-specific adherens junction (AJ) known as the ectoplasmic specialization (ES). ES is an F-actin-rich ultrastructure in which bundles of actin filaments are sandwiched in-between plasma membrane and cisternae of endoplasmic reticulum not found in other mammalian epithelial/endothelial cells. The ES is restricted to the interface of Sertoli cells and spermatids (step 8-19) known as the apical ES, and to the Sertoli cell-cell interface known as the basal ES. Interestingly, the basal ES is also an integrated component of the blood-testis barrier (BTB), coexisting with tight junction (TJ) and gap junction (GJ), and it is conceivable that actin filament bundles at the ES undergo extensive organization, converting from their "bundled" to "de-bundled/branching" configuration to facilitate transport of germ cells across the epithelium and at the BTB during the epithelial cycle. A recent report (Lie et al. PNAS 109:12562-12567, 2012) has demonstrated that the stage-specific and spatiotemporal expression of p-FAK-Tyr(407) and -Tyr(397) are crucial to the regulation of these events via their stage-specific and spatiotemporal expression during the epithelial cycle mediated by their effects on the organization of the actin filament bundles at the ES, involving actin binding/regulatory proteins. In this Commentary, we will critically evaluate these findings in light of other recent reports in the field. While these ideas are based on studies in the BTB in the rat testis, this information should be applicable and helpful to investigators studying other tissue barriers.
Language	English
Publishing date	2014-02-09
Publishing country	United States
Document type	Journal Article
ISSN	2168-8362
ISSN	2168-8362
DOI	10.4161/tisb.24252
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Article ; Online: Crosstalk between desmoglein-2/desmocollin-2/Src kinase and coxsackie and adenovirus receptor/ZO-1 protein complexes, regulates blood-testis barrier dynamics.

Lie, Pearl P Y / Cheng, C Yan / Mruk, Dolores D

The international journal of biochemistry & cell biology

2010 Volume 42, Issue 6, Page(s) 975–986

Abstract: Morphological studies in the testis reported the presence of 'desmosome-like' junctions between Sertoli cells at the blood-testis barrier, whose function is also constituted by tight junctions and basal ectoplasmic specializations. Unfortunately, little ... ...

Abstract	Morphological studies in the testis reported the presence of 'desmosome-like' junctions between Sertoli cells at the blood-testis barrier, whose function is also constituted by tight junctions and basal ectoplasmic specializations. Unfortunately, little is known about the role of desmosomes in blood-testis barrier dynamics. This study aims to fill this gap with the functional investigation of two desmosomal cadherins, desmoglein-2 and desmocollin-2, by their specific knockdown in Sertoli cells cultured in vitro. Reminiscent of the blood-testis barrier in vivo, desmosome-like structures were visible by electron microscopy when Sertoli cells were cultured at high density, thereby forming a polarized epithelium with functional cell junctions. At this point, we opted to focus our efforts on desmoglein-2 and desmocollin-2 based on results which illustrated desmosomal mRNAs to be expressed by Sertoli and germ cells, as well as on results which illustrated desmoglein-2 to co-immunoprecipitate with plakoglobin, c-Src and desmocollin-2. Simultaneous knockdown of desmoglein-2 and desmocollin-2 not only led to a reduction in and mislocalization of zonula occludens-1, but also perturbed the localization of c-Src and coxsackie and adenovirus receptor at the cell-cell interface, resulting in disruption of tight junction permeability barrier. We hereby propose a novel regulatory protein complex composed of desmoglein-2, desmocollin-2, c-Src, coxsackie and adenovirus receptor and zonula occludens-1 at the blood-testis barrier.
MeSH term(s)	Animals ; Blood-Testis Barrier/metabolism ; Blood-Testis Barrier/pathology ; Capillary Permeability/genetics ; Cells, Cultured ; Desmocollins/genetics ; Desmocollins/metabolism ; Desmoglein 2/genetics ; Desmoglein 2/metabolism ; Desmosomes/genetics ; Desmosomes/metabolism ; Desmosomes/pathology ; Male ; Membrane Proteins/metabolism ; Multiprotein Complexes/metabolism ; Phosphoproteins/metabolism ; Protein Transport/genetics ; RNA, Small Interfering/genetics ; Rats ; Rats, Sprague-Dawley ; Receptors, Cytoplasmic and Nuclear/metabolism ; Sertoli Cells/metabolism ; Sertoli Cells/pathology ; Tight Junctions/pathology ; Zonula Occludens-1 Protein ; src-Family Kinases/metabolism
Chemical Substances	Desmocollins ; Desmoglein 2 ; Membrane Proteins ; Multiprotein Complexes ; Phosphoproteins ; RNA, Small Interfering ; Receptors, Cytoplasmic and Nuclear ; Tjp1 protein, rat ; Zonula Occludens-1 Protein ; constitutive androstane receptor (438XLITDI3) ; src-Family Kinases (EC 2.7.10.2)
Language	English
Publishing date	2010-02-25
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1228429-4
ISSN	1878-5875 ; 1357-2725
ISSN (online)	1878-5875
ISSN	1357-2725
DOI	10.1016/j.biocel.2010.02.010
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Zs.A 431: Show issues

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Article: Coordinating cellular events during spermatogenesis: a biochemical model.

Lie, Pearl P Y / Cheng, C Yan / Mruk, Dolores D

Trends in biochemical sciences

2009 Volume 34, Issue 7, Page(s) 366–373

Abstract: Throughout spermatogenesis, a select pool of germ cells, the leptotene spermatocytes, must traverse the blood-testis barrier (BTB) to enter the adluminal compartment of the seminiferous epithelium. This event requires extensive restructuring of cell ... ...

Abstract	Throughout spermatogenesis, a select pool of germ cells, the leptotene spermatocytes, must traverse the blood-testis barrier (BTB) to enter the adluminal compartment of the seminiferous epithelium. This event requires extensive restructuring of cell junctions, and it must also coincide with germ cell cycle progression in preparation for primary spermatocyte meiosis. Recent findings show that cell-cycle-associated kinases and phosphatases, including mitogen-activated protein kinases (MAPKs), participate in the pathways that also direct germ cell adhesion and movement. Our new biochemical model explains, in part, how two distinct cellular events, BTB restructuring and spermiation, are coordinated to maintain spermatogenesis and fertility. In this way, MAPKs would synchronize cell cycle progression in primary spermatocytes with junction remodeling and cell migration across the BTB.
MeSH term(s)	Animals ; Blood-Testis Barrier/physiology ; Cell Cycle/physiology ; Cell Movement/physiology ; Desmosomes/physiology ; Humans ; Intercellular Junctions/physiology ; Male ; Meiotic Prophase I/physiology ; Models, Biological ; Phosphoprotein Phosphatases/metabolism ; Protein Kinases/metabolism ; Spermatogenesis/physiology
Chemical Substances	Protein Kinases (EC 2.7.-) ; Phosphoprotein Phosphatases (EC 3.1.3.16)
Language	English
Publishing date	2009-06-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	194216-5
ISSN	1362-4326 ; 0968-0004 ; 0376-5067
ISSN (online)	1362-4326
ISSN	0968-0004 ; 0376-5067
DOI	10.1016/j.tibs.2009.03.005
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Zs.A 1207: Show issues

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Article: The biology of the desmosome-like junction a versatile anchoring junction and signal transducer in the seminiferous epithelium.

Lie, Pearl P Y / Cheng, C Yan / Mruk, Dolores D

International review of cell and molecular biology

2008 Volume 286, Page(s) 223–269

Abstract: Mammalian spermatogenesis, a complex process that involves the movement of developing germ cells across the seminiferous epithelium, entails extensive restructuring of Sertoli-Sertoli and Sertoli-germ cell junctions. Presently, it is not entirely clear ... ...

Abstract	Mammalian spermatogenesis, a complex process that involves the movement of developing germ cells across the seminiferous epithelium, entails extensive restructuring of Sertoli-Sertoli and Sertoli-germ cell junctions. Presently, it is not entirely clear how zygotene spermatocytes gain entry into the adluminal compartment of the seminiferous epithelium, which is sealed off from the systemic circulation by the Sertoli cell component of the blood-testis barrier, without compromising barrier integrity. To begin to address this question, it is critical that we first have a good understanding of the biology and the regulation of different types of Sertoli-Sertoli and Sertoli-germ cell junctions in the testis. Supported by recent studies in the field, we discuss how crosstalk between different types of junctions contributes to their restructuring during germ cell movement across the blood-testis barrier. We place special emphasis on the emerging role of desmosome-like junctions as signal transducers during germ cell movement across the seminiferous epithelium.
MeSH term(s)	Adherens Junctions/physiology ; Animals ; Desmosomes/physiology ; Germ Cells/metabolism ; Humans ; Intercellular Junctions/physiology ; Male ; Seminiferous Epithelium/physiology ; Sertoli Cells/metabolism ; Signal Transduction
Language	English
Publishing date	2008-01-04
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2427220-6
ISSN	1937-6448 ; 0074-7696
ISSN	1937-6448 ; 0074-7696
DOI	10.1016/B978-0-12-385859-7.00005-7
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