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Article ; Online: Maya Schuldiner.

Schuldiner, Maya

2017 Volume 27, Issue 18, Page(s) R982–R984

Abstract: Interview with Maya Schuldiner, who studies the cell biology of organelles at the Weizmann ...

Abstract	Interview with Maya Schuldiner, who studies the cell biology of organelles at the Weizmann Institute in Israel.
MeSH term(s)	Animals ; Cell Biology/history ; History, 20th Century ; History, 21st Century ; Israel ; Yeasts/cytology
Language	English
Publishing date	2017-09-25
Publishing country	England
Document type	Biography ; Historical Article ; Interview ; Portrait
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2017.07.066
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Article ; Online: Cell scientist to watch--Maya Schuldiner.

Schuldiner, Maya / Bobrowska, Anna

Journal of cell science

2015 Volume 128, Issue 22, Page(s) 4029–4031

Abstract: Maya Schuldiner pursued her PhD degree under the guidance of Prof. Nissim Benvenisty at the Hebrew ... Program and the Sandler Fellows Program. Since 2008, Maya has been running her own laboratory ...

Abstract	Maya Schuldiner pursued her PhD degree under the guidance of Prof. Nissim Benvenisty at the Hebrew University in Jerusalem. She carried out her postdoctoral training in the laboratory of Prof. Jonathan Weissman at the University of California, San Francisco, with support from the Human Frontiers Science Program and the Sandler Fellows Program. Since 2008, Maya has been running her own laboratory at the Weizmann Institute of Sciences in Rehovot, Israel. She received the Human Frontiers Science Program Career Development Award and the NIH Pathway to Independence Award, and she is a member of the EMBO Young Investigator programme and Faculty of 1000. Her current research interests are focused on unravelling novel functions of yeast proteins that are involved in organelle biology.
MeSH term(s)	Animals ; Cell Biology/history ; Faculty, Medical ; Female ; History, 21st Century ; Humans ; Portraits as Topic
Language	English
Publishing date	2015-11-15
Publishing country	England
Document type	Historical Article ; Interview ; Portraits
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.180869
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Article ; Online: Beyond rare disorders: A new era for peroxisomal pathophysiology.

Zalckvar, Einat / Schuldiner, Maya

Molecular cell

2022 Volume 82, Issue 12, Page(s) 2228–2235

Abstract: Metabolism is emerging as a central influencer of multiple disease states in humans. Peroxisomes are central metabolic organelles whose decreased function gives rise to severe peroxisomal diseases. Recently, it is becoming clear that, beyond such rare ... ...

Abstract	Metabolism is emerging as a central influencer of multiple disease states in humans. Peroxisomes are central metabolic organelles whose decreased function gives rise to severe peroxisomal diseases. Recently, it is becoming clear that, beyond such rare inborn errors, the deterioration of peroxisomal functions contributes to multiple and prevalent diseases such as cancer, viral infection, diabetes, and neurodegeneration. Despite the clear importance of peroxisomes in common pathophysiological processes, research on the mechanisms underlying their contributions is still sparse. Here, we highlight the timeliness of focusing on peroxisomes in current research on central, abundant, and society-impacting human pathologies. As peroxisomes are now coming into the spotlight, it is clear that intensive research into these important organelles will enable a better understanding of their contribution to human health, serving as the basis to develop new diagnostic and therapeutic approaches to prevent and treat human diseases.
MeSH term(s)	Humans ; Peroxisomal Disorders/diagnosis ; Peroxisomal Disorders/genetics ; Peroxisomal Disorders/metabolism ; Peroxisomes/metabolism
Language	English
Publishing date	2022-06-09
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2022.05.028
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Article ; Online: A systematic proximity ligation approach to studying protein-substrate specificity identifies the substrate spectrum of the Ssh1 translocon.

Cohen, Nir / Aviram, Naama / Schuldiner, Maya

The EMBO journal

2023 Volume 42, Issue 11, Page(s) e113385

Abstract: Many cellular functions are carried out by protein pairs or families, providing robustness alongside functional diversity. For such processes, it remains a challenge to map the degree of specificity versus promiscuity. Protein-protein interactions (PPIs) ...

Abstract	Many cellular functions are carried out by protein pairs or families, providing robustness alongside functional diversity. For such processes, it remains a challenge to map the degree of specificity versus promiscuity. Protein-protein interactions (PPIs) can be used to inform on these matters as they highlight cellular locals, regulation and, in cases where proteins affect other proteins - substrate range. However, methods to systematically study transient PPIs are underutilized. In this study, we create a novel approach to systematically compare stable or transient PPIs between two yeast proteins. Our approach, Cel-lctiv (CELlular biotin-Ligation for Capturing Transient Interactions in vivo), uses high-throughput pairwise proximity biotin ligation for comparing PPIs systematically and in vivo. As a proof of concept, we studied the homologous translocation pores Sec61 and Ssh1. We show how Cel-lctiv can uncover the unique substrate range for each translocon allowing us to pinpoint a specificity determinator driving interaction preference. More generally, this demonstrates how Cel-lctiv can provide direct information on substrate specificity even for highly homologous proteins.
MeSH term(s)	Humans ; Biotin ; Phosphoprotein Phosphatases ; Substrate Specificity ; Saccharomyces cerevisiae Proteins
Chemical Substances	Biotin (6SO6U10H04) ; Phosphoprotein Phosphatases (EC 3.1.3.16) ; Saccharomyces cerevisiae Proteins ; SSH1 protein, S cerevisiae
Language	English
Publishing date	2023-04-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.2022113385
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Article ; Online: Show your true color: Mammalian cell surface staining for tracking cellular identity in multiplexing and beyond.

Hassdenteufel, Sarah / Schuldiner, Maya

Current opinion in chemical biology

2021 Volume 66, Page(s) 102102

Abstract: Fluorescence microscopy revolutionized cell biology and changed requirements for dyes towards higher brightness, novel capacities, and specific targets. With the need for multiplexing assays in high-throughput methodologies, surface staining gained ... ...

Abstract	Fluorescence microscopy revolutionized cell biology and changed requirements for dyes towards higher brightness, novel capacities, and specific targets. With the need for multiplexing assays in high-throughput methodologies, surface staining gained particular interest because it allows rapid application of exogenous stains to track cellular identity in mixed populations. Indeed, the last decade has enriched the toolbox of general lipid stains, fluorescent lipid analogues, sugar-binding lectins, and protein-specific antibodies enabling the first rationally designed plasma membrane-specific dyes. Still, multiple challenges exist, and the unique properties of each dye must be considered when selecting a staining approach for a specific application. Recent advances are also promising that future dyes will provide ultimate brightness and photostability in diverse colors and reduced sizes for high-resolution imaging.
MeSH term(s)	Animals ; Cell Membrane/metabolism ; Fluorescent Dyes/chemistry ; Mammals ; Microscopy, Fluorescence/methods ; Staining and Labeling
Chemical Substances	Fluorescent Dyes
Language	English
Publishing date	2021-11-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1439176-4
ISSN	1879-0402 ; 1367-5931
ISSN (online)	1879-0402
ISSN	1367-5931
DOI	10.1016/j.cbpa.2021.102102
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Article ; Online: A Similarity-Based Method for Predicting Enzymatic Functions in Yeast Uncovers a New AMP Hydrolase.

Cohen, Nir / Kahana, Amit / Schuldiner, Maya

Journal of molecular biology

2022 Volume 434, Issue 7, Page(s) 167478

Abstract: Despite decades of research and the availability of the full genomic sequence of the baker's yeast Saccharomyces cerevisiae, still a large fraction of its genome is not functionally annotated. This hinders our ability to fully understand cellular ... ...

Abstract	Despite decades of research and the availability of the full genomic sequence of the baker's yeast Saccharomyces cerevisiae, still a large fraction of its genome is not functionally annotated. This hinders our ability to fully understand cellular activity and suggests that many additional processes await discovery. The recent years have shown an explosion of high-quality genomic and structural data from multiple organisms, ranging from bacteria to mammals. New computational methods now allow us to integrate these data and extract meaningful insights into the functional identity of uncharacterized proteins in yeast. Here, we created a database of sensitive sequence similarity predictions for all yeast proteins. We use this information to identify candidate enzymes for known biochemical reactions whose enzymes are unidentified, and show how this provides a powerful basis for experimental validation. Using one pathway as a test case we pair a new function for the previously uncharacterized enzyme Yhr202w, as an extra-cellular AMP hydrolase in the NAD degradation pathway. Yhr202w, which we now term Smn1 for Scavenger MonoNucleotidase 1, is a highly conserved protein that is similar to the human protein E5NT/CD73, which is associated with multiple cancers. Hence, our new methodology provides a paradigm, that can be adopted to other organisms, for uncovering new enzymatic functions of uncharacterized proteins.
MeSH term(s)	Humans ; Adenosine Monophosphate/chemistry ; Nucleotidases/chemistry ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae Proteins/chemistry ; Sequence Analysis, Protein/methods
Chemical Substances	Adenosine Monophosphate (415SHH325A) ; Nucleotidases (EC 3.1.3.-) ; Saccharomyces cerevisiae Proteins ; YHR202W protein, S cerevisiae (EC 3.1.26.5)
Language	English
Publishing date	2022-02-03
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2022.167478
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Article: Beyond rare disorders: A new era for peroxisomal pathophysiology

Zalckvar, Einat / Schuldiner, Maya

Molecular cell. 2022 June 16, v. 82, no. 12

2022

Abstract	Metabolism is emerging as a central influencer of multiple disease states in humans. Peroxisomes are central metabolic organelles whose decreased function gives rise to severe peroxisomal diseases. Recently, it is becoming clear that, beyond such rare inborn errors, the deterioration of peroxisomal functions contributes to multiple and prevalent diseases such as cancer, viral infection, diabetes, and neurodegeneration. Despite the clear importance of peroxisomes in common pathophysiological processes, research on the mechanisms underlying their contributions is still sparse. Here, we highlight the timeliness of focusing on peroxisomes in current research on central, abundant, and society-impacting human pathologies. As peroxisomes are now coming into the spotlight, it is clear that intensive research into these important organelles will enable a better understanding of their contribution to human health, serving as the basis to develop new diagnostic and therapeutic approaches to prevent and treat human diseases.
Keywords	diabetes ; human health ; humans ; metabolism ; neurodegenerative diseases ; pathophysiology ; peroxisomes ; therapeutics
Language	English
Dates of publication	2022-0616
Size	p. 2228-2235.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2022.05.028
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Article ; Online: New horizons in mitochondrial contact site research.

Zung, Naama / Schuldiner, Maya

Biological chemistry

2020 Volume 401, Issue 6-7, Page(s) 793–809

Abstract: Contact sites, areas where two organelles are held in close proximity through the action of molecular tethers, enable non-vesicular communication between compartments. Mitochondria have been center stage in the contact site field since the discovery of ... ...

Abstract	Contact sites, areas where two organelles are held in close proximity through the action of molecular tethers, enable non-vesicular communication between compartments. Mitochondria have been center stage in the contact site field since the discovery of the first contact between mitochondria and the endoplasmic reticulum (ER) over 60 years ago. However, only now, in the last decade, has there been a burst of discoveries regarding contact site biology in general and mitochondrial contacts specifically. The number and types of characterized contacts increased dramatically, new molecular mechanisms enabling contact formation were discovered, additional unexpected functions for contacts were shown, and their roles in cellular and organismal physiology were emphasized. Here, we focus on mitochondria as we highlight the most recent developments, future goals and unresolved questions in the field.
MeSH term(s)	Animals ; Endoplasmic Reticulum/metabolism ; Humans ; Mitochondria/metabolism ; Saccharomyces cerevisiae/metabolism
Language	English
Publishing date	2020-04-23
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1334659-3
ISSN	1437-4315 ; 1431-6730 ; 1432-0355
ISSN (online)	1437-4315
ISSN	1431-6730 ; 1432-0355
DOI	10.1515/hsz-2020-0133
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Article ; Online: Spindle Position Checkpoint Kinase Kin4 Regulates Organelle Transport in

Ekal, Lakhan / Alqahtani, Abdulaziz M S / Schuldiner, Maya / Zalckvar, Einat / Hettema, Ewald H / Ayscough, Kathryn R

Biomolecules

2023 Volume 13, Issue 7

Abstract: Membrane-bound organelles play important, frequently essential, roles in cellular metabolism in eukaryotes. Hence, cells have evolved molecular mechanisms to closely monitor organelle dynamics and maintenance. The actin cytoskeleton plays a vital role in ...

Abstract	Membrane-bound organelles play important, frequently essential, roles in cellular metabolism in eukaryotes. Hence, cells have evolved molecular mechanisms to closely monitor organelle dynamics and maintenance. The actin cytoskeleton plays a vital role in organelle transport and positioning across all eukaryotes. Studies in the budding yeast
MeSH term(s)	Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Protein Serine-Threonine Kinases/metabolism ; Protein Kinases/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Actomyosin/metabolism ; Mitosis ; Spindle Apparatus/metabolism ; Organelles
Chemical Substances	Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Protein Kinases (EC 2.7.-) ; Saccharomyces cerevisiae Proteins ; Actomyosin (9013-26-7)
Language	English
Publishing date	2023-07-10
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom13071098
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Article ; Online: The Fast and the Furious: Golgi Contact Sites.

David, Yotam / Castro, Inês G / Schuldiner, Maya

Contact (Thousand Oaks (Ventura County, Calif.))

2021 Volume 4, Page(s) 1–15

Abstract: Contact sites are areas of close apposition between two membranes that coordinate nonvesicular communication between organelles. Such interactions serve a wide range of cellular functions from regulating metabolic pathways to executing stress responses ... ...

Abstract	Contact sites are areas of close apposition between two membranes that coordinate nonvesicular communication between organelles. Such interactions serve a wide range of cellular functions from regulating metabolic pathways to executing stress responses and coordinating organelle inheritance. The past decade has seen a dramatic increase in information on certain contact sites, mostly those involving the endoplasmic reticulum. However, despite its central role in the secretory pathway, the Golgi apparatus and its contact sites remain largely unexplored. In this review, we discuss the current knowledge of Golgi contact sites and share our thoughts as to why Golgi contact sites are understudied. We also highlight what exciting future directions may exist in this emerging field.
Language	English
Publishing date	2021-08-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	2964312-0
ISSN	2515-2564 ; 2515-2564
ISSN (online)	2515-2564
ISSN	2515-2564
DOI	10.1177/25152564211034424
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