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Article: Editorial: Energy Requirements in Membrane Trafficking.

Guardia, Carlos M / Hierro, Aitor / Gershlick, David C

Frontiers in cell and developmental biology

2021 Volume 9, Page(s) 750633

Language	English
Publishing date	2021-10-14
Publishing country	Switzerland
Document type	Editorial
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2021.750633
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Article ; Online: Measurement of Lysosome Positioning by Shell Analysis and Line Scan.

Williamson, Chad D / Guardia, Carlos M / De Pace, Raffaella / Bonifacino, Juan S / Saric, Amra

Methods in molecular biology (Clifton, N.J.)

2022 Volume 2473, Page(s) 285–306

Abstract: Lysosomes are membrane-bound organelles that degrade diverse biomolecules and regulate a multitude of other essential processes including cell growth and metabolism, signaling, plasma membrane repair and infection. Such diverse functions of lysosomes are ...

Abstract	Lysosomes are membrane-bound organelles that degrade diverse biomolecules and regulate a multitude of other essential processes including cell growth and metabolism, signaling, plasma membrane repair and infection. Such diverse functions of lysosomes are highly coordinated in space and time and are therefore tightly coupled to the directional transport of the organelles within the cytoplasm. Thus, robust quantitative assessments of lysosome positioning within the cell provide a valuable tool for researchers interested in understanding these multifunctional organelles. Here, we present point-by-point methodology to measure lysosome positioning by two straight forward and widely used techniques: shell analysis and line scan.
MeSH term(s)	Lysosomes/metabolism ; Signal Transduction
Language	English
Publishing date	2022-07-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-2209-4_19
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Article ; Online: The power of peer networking for improving STEM faculty job applications: a successful pilot programme.

Guardia, Carlos M / Kane, Erin / Tebo, Alison G / Sanders, Anna A W M / Kaya, Devrim / Grogan, Kathleen E

Proceedings. Biological sciences

2023 Volume 290, Issue 1997, Page(s) 20230124

Abstract: To attain a faculty position, postdoctoral fellows submit job applications that require considerable time and effort to produce. Although mentors and colleagues review these applications, postdocs rarely receive iterative feedback from reviewers with the ...

Abstract	To attain a faculty position, postdoctoral fellows submit job applications that require considerable time and effort to produce. Although mentors and colleagues review these applications, postdocs rarely receive iterative feedback from reviewers with the breadth of expertise typically found on an academic search committee. To address this gap, we describe an international peer-reviewing programme for postdocs across disciplines to receive reciprocal, iterative feedback on faculty applications. A participant survey revealed that nearly all participants would recommend the programme to others. Furthermore, our programme was more likely to attract postdocs who struggled to find mentoring, possibly because of their identity as a woman or member of an underrepresented population in STEM or because they changed fields. Between 2018 and 2021, our programme provided nearly 150 early career academics with a diverse and supportive community of peer mentors during the difficult search for a faculty position and continues to do so today. As the transition from postdoc to faculty represents the largest 'leak' in the academic pipeline, implementation of similar programmes by universities or professional societies would provide psycho-social support necessary to prevent attrition of individuals from underrepresented populations as well as increase the chances of success for early career academics in their search for independence.
MeSH term(s)	Female ; Humans ; Pilot Projects ; Mentoring ; Mentors ; Faculty ; Peer Group
Language	English
Publishing date	2023-04-26
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	209242-6
ISSN	1471-2954 ; 0080-4649 ; 0962-8452 ; 0950-1193
ISSN (online)	1471-2954
ISSN	0080-4649 ; 0962-8452 ; 0950-1193
DOI	10.1098/rspb.2023.0124
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Zs.A 1364: Show issues

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Article ; Online: RUSC2 and WDR47 oppositely regulate kinesin-1-dependent distribution of ATG9A to the cell periphery.

Guardia, Carlos M / Jain, Akansha / Mattera, Rafael / Friefeld, Alex / Li, Yan / Bonifacino, Juan S

Molecular biology of the cell

2021 Volume 32, Issue 21, Page(s) ar25

Abstract: Autophagy-related protein 9 (ATG9) is a transmembrane protein component of the autophagy machinery that cycles between ... ...

Abstract	Autophagy-related protein 9 (ATG9) is a transmembrane protein component of the autophagy machinery that cycles between the
MeSH term(s)	Autophagosomes/metabolism ; Autophagy ; Autophagy-Related Proteins/metabolism ; Carrier Proteins/metabolism ; Carrier Proteins/physiology ; HEK293 Cells ; HeLa Cells ; Humans ; Kinesins/metabolism ; Membrane Proteins/metabolism ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism ; Nerve Tissue Proteins/metabolism ; Protein Transport/physiology ; Vesicular Transport Proteins/metabolism ; trans-Golgi Network/metabolism
Chemical Substances	ATG9A protein, human ; Autophagy-Related Proteins ; Carrier Proteins ; KIF5B protein, human ; Membrane Proteins ; Microtubule-Associated Proteins ; Nerve Tissue Proteins ; RUSC2 protein, human ; Vesicular Transport Proteins ; WDR47 protein, human ; Kinesins (EC 3.6.4.4)
Language	English
Publishing date	2021-08-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E21-06-0295
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Zs.A 2853: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: A neurodevelopmental disorder associated with an activating de novo missense variant in ARF1.

Ishida, Morié / Otero, María G / Freeman, Christina / Sánchez-Lara, Pedro A / Guardia, Carlos M / Pierson, Tyler Mark / Bonifacino, Juan S

Human molecular genetics

2022 Volume 32, Issue 7, Page(s) 1162–1174

Abstract: ADP-ribosylation factor 1 (ARF1) is a small GTPase that regulates membrane traffic at the Golgi apparatus and endosomes through recruitment of several coat proteins and lipid-modifying enzymes. Here, we report a pediatric patient with an ARF1-related ... ...

Abstract	ADP-ribosylation factor 1 (ARF1) is a small GTPase that regulates membrane traffic at the Golgi apparatus and endosomes through recruitment of several coat proteins and lipid-modifying enzymes. Here, we report a pediatric patient with an ARF1-related disorder because of a monoallelic de novo missense variant (c.296 G > A; p.R99H) in the ARF1 gene, associated with developmental delay, hypotonia, intellectual disability and motor stereotypies. Neuroimaging revealed a hypoplastic corpus callosum and subcortical white matter abnormalities. Notably, this patient did not exhibit periventricular heterotopias previously observed in other patients with ARF1 variants (including p.R99H). Functional analysis of the R99H-ARF1 variant protein revealed that it was expressed at normal levels and properly localized to the Golgi apparatus; however, the expression of this variant caused swelling of the Golgi apparatus, increased the recruitment of coat proteins such as coat protein complex I, adaptor protein complex 1 and GGA3 and altered the morphology of recycling endosomes. In addition, we observed that the expression of R99H-ARF1 prevented dispersal of the Golgi apparatus by the ARF1-inhibitor brefeldin A. Finally, protein interaction analyses showed that R99H-ARF1 bound more tightly to the ARF1-effector GGA3 relative to wild-type ARF1. These properties were similar to those of the well-characterized constitutively active Q71L-ARF1 mutant, indicating that the pathogenetic mechanism of the R99H-ARF1 variant involves constitutive activation with resultant Golgi and endosomal alterations. The absence of periventricular nodular heterotopias in this R99H-ARF1 subject also indicates that this finding may not be a consistent phenotypic expression of all ARF1-related disorders.
MeSH term(s)	Humans ; Animals ; Mice ; ADP-Ribosylation Factor 1/chemistry ; ADP-Ribosylation Factor 1/genetics ; ADP-Ribosylation Factor 1/metabolism ; Mutation, Missense ; Female ; Child ; Golgi Apparatus/pathology ; Endosomes/pathology ; Neurodevelopmental Disorders/diagnosis ; Neurodevelopmental Disorders/genetics ; Neurodevelopmental Disorders/pathology
Chemical Substances	ARF1 protein, human (EC 3.6.5.2) ; ADP-Ribosylation Factor 1 (EC 3.6.5.2)
Language	English
Publishing date	2022-11-07
Publishing country	England
Document type	Case Reports ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Intramural
ZDB-ID	1108742-0
ISSN	1460-2083 ; 0964-6906
ISSN (online)	1460-2083
ISSN	0964-6906
DOI	10.1093/hmg/ddac279
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Zs.A 3469: Show issues

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Article ; Online: Transcytosis and trans-synaptic retention by postsynaptic ErbB4 underlie axonal accumulation of NRG3.

Ahmad, Tanveer / Vullhorst, Detlef / Chaudhuri, Rituparna / Guardia, Carlos M / Chaudhary, Nisha / Karavanova, Irina / Bonifacino, Juan S / Buonanno, Andres

The Journal of cell biology

2022 Volume 221, Issue 7

Abstract: Neuregulins (NRGs) are EGF-like ligands associated with cognitive disorders. Unprocessed proNRG3 is cleaved by BACE1 to generate the mature membrane-bound NRG3 ligand, but the subcellular site of proNRG3 cleavage, mechanisms underlying its transport into ...

Abstract	Neuregulins (NRGs) are EGF-like ligands associated with cognitive disorders. Unprocessed proNRG3 is cleaved by BACE1 to generate the mature membrane-bound NRG3 ligand, but the subcellular site of proNRG3 cleavage, mechanisms underlying its transport into axons, and presynaptic accumulation remain unknown. Using an optogenetic proNRG3 cleavage reporter (LA143-NRG3), we investigate the spatial-temporal dynamics of NRG3 processing and sorting in neurons. In dark conditions, unprocessed LA143-NRG3 is retained in the trans-Golgi network but, upon photoactivation, is cleaved by BACE1 and released from the TGN. Mature NRG3 then emerges on the somatodendritic plasma membrane from where it is re-endocytosed and anterogradely transported on Rab4+ vesicles into axons via transcytosis. By contrast, the BACE1 substrate APP is sorted into axons on Rab11+ vesicles. Lastly, by a mechanism we denote "trans-synaptic retention," NRG3 accumulates at presynaptic terminals by stable interaction with its receptor ErbB4 on postsynaptic GABAergic interneurons. We propose that trans-synaptic retention may account for polarized expression of other neuronal transmembrane ligands and receptors.
MeSH term(s)	Amyloid Precursor Protein Secretases/genetics ; Amyloid Precursor Protein Secretases/metabolism ; Animals ; Aspartic Acid Endopeptidases/genetics ; Aspartic Acid Endopeptidases/metabolism ; Axons/metabolism ; HEK293 Cells ; Humans ; Ligands ; Mice ; Neuregulins/genetics ; Neuregulins/metabolism ; Rats ; Receptor, ErbB-4/genetics ; Receptor, ErbB-4/metabolism ; Transcytosis
Chemical Substances	Ligands ; NRG3 protein, human ; Neuregulins ; ERBB4 protein, human (EC 2.7.10.1) ; Receptor, ErbB-4 (EC 2.7.10.1) ; Amyloid Precursor Protein Secretases (EC 3.4.-) ; Aspartic Acid Endopeptidases (EC 3.4.23.-) ; BACE1 protein, human (EC 3.4.23.46)
Language	English
Publishing date	2022-05-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202110167
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Article ; Online: Neuronal functions of adaptor complexes involved in protein sorting.

Guardia, Carlos M / De Pace, Raffaella / Mattera, Rafael / Bonifacino, Juan S

Current opinion in neurobiology

2018 Volume 51, Page(s) 103–110

Abstract: Selective transport of transmembrane proteins to different intracellular compartments often involves the recognition of sorting signals in the cytosolic domains of the proteins by components of membrane coats. Some of these coats have as their key ... ...

Abstract	Selective transport of transmembrane proteins to different intracellular compartments often involves the recognition of sorting signals in the cytosolic domains of the proteins by components of membrane coats. Some of these coats have as their key components a family of heterotetrameric adaptor protein (AP) complexes named AP-1 through AP-5. AP complexes play important roles in all cells, but their functions are most critical in neurons because of the extreme compartmental complexity of these cells. Accordingly, various diseases caused by mutations in AP subunit genes exhibit a range of neurological abnormalities as their most salient features. In this article, we discuss the properties of the different AP complexes, with a focus on their roles in neuronal physiology and pathology.
MeSH term(s)	Action Potentials/genetics ; Adaptor Proteins, Vesicular Transport/genetics ; Adaptor Proteins, Vesicular Transport/metabolism ; Animals ; Humans ; Mutation/genetics ; Nervous System Diseases/genetics ; Neurons/metabolism ; Protein Transport/physiology
Chemical Substances	Adaptor Proteins, Vesicular Transport
Language	English
Publishing date	2018-03-17
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	1078046-4
ISSN	1873-6882 ; 0959-4388
ISSN (online)	1873-6882
ISSN	0959-4388
DOI	10.1016/j.conb.2018.02.021
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Article ; Online: The autophagy protein ATG9A enables lipid mobilization from lipid droplets.

Mailler, Elodie / Guardia, Carlos M / Bai, Xiaofei / Jarnik, Michal / Williamson, Chad D / Li, Yan / Maio, Nunziata / Golden, Andy / Bonifacino, Juan S

Nature communications

2021 Volume 12, Issue 1, Page(s) 6750

Abstract: The multispanning membrane protein ATG9A is a scramblase that flips phospholipids between the two membrane leaflets, thus contributing to the expansion of the phagophore membrane in the early stages of autophagy. Herein, we show that depletion of ATG9A ... ...

Abstract	The multispanning membrane protein ATG9A is a scramblase that flips phospholipids between the two membrane leaflets, thus contributing to the expansion of the phagophore membrane in the early stages of autophagy. Herein, we show that depletion of ATG9A does not only inhibit autophagy but also increases the size and/or number of lipid droplets in human cell lines and C. elegans. Moreover, ATG9A depletion blocks transfer of fatty acids from lipid droplets to mitochondria and, consequently, utilization of fatty acids in mitochondrial respiration. ATG9A localizes to vesicular-tubular clusters (VTCs) that are tightly associated with an ER subdomain enriched in another multispanning membrane scramblase, TMEM41B, and also in close proximity to phagophores, lipid droplets and mitochondria. These findings indicate that ATG9A plays a critical role in lipid mobilization from lipid droplets to autophagosomes and mitochondria, highlighting the importance of ATG9A in both autophagic and non-autophagic processes.
MeSH term(s)	Animals ; Animals, Genetically Modified ; Autophagosomes/metabolism ; Autophagy ; Autophagy-Related Proteins/genetics ; Autophagy-Related Proteins/metabolism ; Caenorhabditis elegans ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Fatty Acids/metabolism ; Gene Knockout Techniques ; HEK293 Cells ; HeLa Cells ; Humans ; Lipid Droplets/metabolism ; Lipid Mobilization ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mitochondria/metabolism ; Mutation ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/metabolism
Chemical Substances	ATG9A protein, human ; Autophagy-Related Proteins ; Caenorhabditis elegans Proteins ; Fatty Acids ; Membrane Proteins ; Recombinant Proteins ; Vesicular Transport Proteins ; atg-9 protein, C elegans
Language	English
Publishing date	2021-11-19
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-26999-x
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Article ; Online: SNX19 restricts endolysosome motility through contacts with the endoplasmic reticulum.

Saric, Amra / Freeman, Spencer A / Williamson, Chad D / Jarnik, Michal / Guardia, Carlos M / Fernandopulle, Michael S / Gershlick, David C / Bonifacino, Juan S

Nature communications

2021 Volume 12, Issue 1, Page(s) 4552

Abstract: The ability of endolysosomal organelles to move within the cytoplasm is essential for the performance of their functions. Long-range movement involves coupling of the endolysosomes to motor proteins that carry them along microtubule tracks. This movement ...

Abstract	The ability of endolysosomal organelles to move within the cytoplasm is essential for the performance of their functions. Long-range movement involves coupling of the endolysosomes to motor proteins that carry them along microtubule tracks. This movement is influenced by interactions with other organelles, but the mechanisms involved are incompletely understood. Herein we show that the sorting nexin SNX19 tethers endolysosomes to the endoplasmic reticulum (ER), decreasing their motility and contributing to their concentration in the perinuclear area of the cell. Tethering depends on two N-terminal transmembrane domains that anchor SNX19 to the ER, and a PX domain that binds to phosphatidylinositol 3-phosphate on the endolysosomal membrane. Two other domains named PXA and PXC negatively regulate the interaction of SNX19 with endolysosomes. These studies thus identify a mechanism for controlling the motility and positioning of endolysosomes that involves tethering to the ER by a sorting nexin.
MeSH term(s)	Cell Line, Tumor ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum/ultrastructure ; Endosomes/metabolism ; Endosomes/ultrastructure ; Humans ; Lysosomes/metabolism ; Lysosomes/ultrastructure ; Phosphatidylinositol Phosphates/metabolism ; Protein Binding ; Protein Domains ; Protein Transport ; Sorting Nexins/chemistry ; Sorting Nexins/metabolism
Chemical Substances	Phosphatidylinositol Phosphates ; SNX19 protein, human ; Sorting Nexins ; phosphatidylinositol 3-phosphate
Language	English
Publishing date	2021-07-27
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-24709-1
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Article: Mechanisms of Polarized Organelle Distribution in Neurons.

Britt, Dylan J / Farías, Ginny G / Guardia, Carlos M / Bonifacino, Juan S

Frontiers in cellular neuroscience

2016 Volume 10, Page(s) 88

Abstract: Neurons are highly polarized cells exhibiting axonal and somatodendritic domains with distinct complements of cytoplasmic organelles. Although some organelles are widely distributed throughout the neuronal cytoplasm, others are segregated to either the ... ...

Abstract	Neurons are highly polarized cells exhibiting axonal and somatodendritic domains with distinct complements of cytoplasmic organelles. Although some organelles are widely distributed throughout the neuronal cytoplasm, others are segregated to either the axonal or somatodendritic domains. Recent findings show that organelle segregation is largely established at a pre-axonal exclusion zone (PAEZ) within the axon hillock. Polarized sorting of cytoplasmic organelles at the PAEZ is proposed to depend mainly on their selective association with different microtubule motors and, in turn, with distinct microtubule arrays. Somatodendritic organelles that escape sorting at the PAEZ can be subsequently retrieved at the axon initial segment (AIS) by a microtubule- and/or actin-based mechanism. Dynamic sorting along the PAEZ-AIS continuum can thus explain the polarized distribution of cytoplasmic organelles between the axonal and somatodendritic domains.
Language	English
Publishing date	2016-03-31
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2452963-1
ISSN	1662-5102
ISSN	1662-5102
DOI	10.3389/fncel.2016.00088
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