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Article ; Online: A two-kinesin mechanism controls neurogenesis in the developing brain.

Helmer, Paige / Vallee, Richard B

Communications biology

2023 Volume 6, Issue 1, Page(s) 1219

Abstract: During the course of brain development, Radial Glial Progenitor (RGP) cells give rise to most of the neurons required for a functional cortex. RGPs can undergo symmetric divisions, which result in RGP duplication, or asymmetric divisions, which result in ...

Abstract	During the course of brain development, Radial Glial Progenitor (RGP) cells give rise to most of the neurons required for a functional cortex. RGPs can undergo symmetric divisions, which result in RGP duplication, or asymmetric divisions, which result in one RGP as well as one to four neurons. The control of this balance is not fully understood, but must be closely regulated to produce the cells required for a functioning cortex, and to maintain the stem cell pool. In this study, we show that the balance between symmetric and asymmetric RGP divisions is in part regulated by the actions of two kinesins, Kif1A and Kif13B, which we find have opposing roles in neurogenesis through their action on the mitotic spindle in dividing RGPs. We find that Kif1A promotes neurogenesis, whereas Kif13B promotes symmetric, non-neurogenic divisions. Interestingly, the two kinesins are closely related in structure, and members of the same kinesin-3 subfamily, thus their opposing effects on spindle orientation appear to represent a novel mechanism for the regulation of neurogenesis.
MeSH term(s)	Kinesins/genetics ; Kinesins/metabolism ; Neurons/metabolism ; Neurogenesis/physiology ; Cerebral Cortex/metabolism ; Stem Cells/metabolism
Chemical Substances	Kinesins (EC 3.6.4.4)
Language	English
Publishing date	2023-12-01
Publishing country	England
Document type	Journal Article
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-023-05604-5
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: A two-kinesin mechanism controls neurogenesis in the developing brain

Paige Helmer / Richard B. Vallee

Communications Biology, Vol 6, Iss 1, Pp 1-

2023 Volume 10

Abstract: Abstract During the course of brain development, Radial Glial Progenitor (RGP) cells give rise to most of the neurons required for a functional cortex. RGPs can undergo symmetric divisions, which result in RGP duplication, or asymmetric divisions, which ... ...

Abstract	Abstract During the course of brain development, Radial Glial Progenitor (RGP) cells give rise to most of the neurons required for a functional cortex. RGPs can undergo symmetric divisions, which result in RGP duplication, or asymmetric divisions, which result in one RGP as well as one to four neurons. The control of this balance is not fully understood, but must be closely regulated to produce the cells required for a functioning cortex, and to maintain the stem cell pool. In this study, we show that the balance between symmetric and asymmetric RGP divisions is in part regulated by the actions of two kinesins, Kif1A and Kif13B, which we find have opposing roles in neurogenesis through their action on the mitotic spindle in dividing RGPs. We find that Kif1A promotes neurogenesis, whereas Kif13B promotes symmetric, non-neurogenic divisions. Interestingly, the two kinesins are closely related in structure, and members of the same kinesin-3 subfamily, thus their opposing effects on spindle orientation appear to represent a novel mechanism for the regulation of neurogenesis.
Keywords	Biology (General) ; QH301-705.5
Subject code	572
Language	English
Publishing date	2023-12-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: A RILP-regulated pathway coordinating autophagosome biogenesis with transport.

Khobrekar, Noopur V / Vallee, Richard B

Autophagy

2020 Volume 16, Issue 8, Page(s) 1537–1538

Abstract: Mammalian cells, including neurons, use macroautophagy (here 'autophagy') to degrade damaged proteins and organelles, and recycle nutrients in response to starvation and other forms of cell stress. The basic cellular machinery responsible for autophagy ... ...

Abstract	Mammalian cells, including neurons, use macroautophagy (here 'autophagy') to degrade damaged proteins and organelles, and recycle nutrients in response to starvation and other forms of cell stress. The basic cellular machinery responsible for autophagy is highly conserved from yeast to mammals. However, evidence for specific adaptations to more complex organisms and in highly differentiated cells (e. g. neurons) remains limited. RILP (Rab interacting lysosomal protein) mediates retrograde transport of late endosomes (LEs) in nonneuronal mammalian cells. We have now found that RILP plays additional important, fundamental roles in neuronal autophagosome (AP) transport, and, more surprisingly, in AP biogenesis, and cargo turnover as well. RILP accomplishes these tasks via sequential interactions with key autophagosomal components - ATG5 and LC3 - as well as the microtubule motor protein cytoplasmic dynein (Figure 1A). We found further that RILP expression and behavior are controlled by MTOR kinase, linking RILP to a potentially wide range of physiological and pathophysiological functions.
Language	English
Publishing date	2020-06-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2020.1778294
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Book: Molecular motors and the cytoskeleton / B

Vallee, Richard B.

(Methods in enzymology ; 298)

1998

Author's details	ed. by Richard B. Vallee
Series title	Methods in enzymology ; 298 Molecular motors and the cytoskeleton
Collection	Molecular motors and the cytoskeleton
Language	English
Size	XXXII, 636 S. : Ill., graph. Darst.
Publisher	Academic Press
Publishing place	San Diego u.a.
Publishing country	United States
Document type	Book
HBZ-ID	HT009058420
ISBN	0-12-182199-4 ; 978-0-12-182199-9
Database	Catalogue ZB MED Medicine, Health

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Se 222 -298-	verfügbar in Königswinter	Königswinter

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Article ; Online: Role of Nesprin-2 and RanBP2 in BICD2-associated brain developmental disorders.

Yi, Julie / Zhao, Xiaoxin / Noell, Crystal R / Helmer, Paige / Solmaz, Sozanne R / Vallee, Richard B

PLoS genetics

2023 Volume 19, Issue 3, Page(s) e1010642

Abstract: Bicaudal D2 (BICD2) is responsible for recruiting cytoplasmic dynein to diverse forms of subcellular cargo for their intracellular transport. Mutations in the human BICD2 gene have been found to cause an autosomal dominant form of spinal muscular atrophy ...

Abstract	Bicaudal D2 (BICD2) is responsible for recruiting cytoplasmic dynein to diverse forms of subcellular cargo for their intracellular transport. Mutations in the human BICD2 gene have been found to cause an autosomal dominant form of spinal muscular atrophy (SMA-LED2), and brain developmental defects. Whether and how the latter mutations are related to roles we and others have identified for BICD2 in brain development remains little understood. BICD2 interacts with the nucleoporin RanBP2 to recruit dynein to the nuclear envelope (NE) of Radial Glial Progenitor cells (RGPs) to mediate their well-known but mysterious cell-cycle-regulated interkinetic nuclear migration (INM) behavior, and their subsequent differentiation to form cortical neurons. We more recently found that BICD2 also mediates NE dynein recruitment in migrating post-mitotic neurons, though via a different interactor, Nesprin-2. Here, we report that Nesprin-2 and RanBP2 compete for BICD2-binding in vitro. To test the physiological implications of this behavior, we examined the effects of known BICD2 mutations using in vitro biochemical and in vivo electroporation-mediated brain developmental assays. We find a clear relationship between the ability of BICD2 to bind RanBP2 vs. Nesprin-2 in controlling of nuclear migration and neuronal migration behavior. We propose that mutually exclusive RanBP2-BICD2 vs. Nesprin-2-BICD2 interactions at the NE play successive, critical roles in INM behavior in RGPs and in post-mitotic neuronal migration and errors in these processes contribute to specific human brain malformations.
MeSH term(s)	Child ; Humans ; Brain/metabolism ; Developmental Disabilities ; Dyneins/metabolism ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Nuclear Pore Complex Proteins/genetics ; Nuclear Pore Complex Proteins/metabolism ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism
Chemical Substances	BICD2 protein, human ; Dyneins (EC 3.6.4.2) ; Microtubule-Associated Proteins ; Nuclear Pore Complex Proteins ; SYNE2 protein, human ; ran-binding protein 2 ; Nerve Tissue Proteins ; Microfilament Proteins ; Molecular Chaperones
Language	English
Publishing date	2023-03-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1010642
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Cdk1 phosphorylation of the dynein adapter Nde1 controls cargo binding from G2 to anaphase.

Wynne, Caitlin L / Vallee, Richard B

The Journal of cell biology

2018 Volume 217, Issue 9, Page(s) 3019–3029

Abstract: Cytoplasmic dynein is involved in diverse cell cycle-dependent functions regulated by several accessory factors, including Nde1 and Ndel1. Little is known about the role of these proteins in dynein cargo binding, and less is known about their cell cycle-- ...

Abstract	Cytoplasmic dynein is involved in diverse cell cycle-dependent functions regulated by several accessory factors, including Nde1 and Ndel1. Little is known about the role of these proteins in dynein cargo binding, and less is known about their cell cycle--dependent dynein regulation. Using Nde1 RNAi, mutant cDNAs, and a phosphorylation site-specific antibody, we found a specific association of phospho-Nde1 with the late G2-M nuclear envelope and prophase to anaphase kinetochores, comparable to the pattern for the Nde1 interactor CENP-F. Phosphomutant-Nde1 associated only with prometaphase kinetochores and showed weaker CENP-F binding in in vitro assays. Nde1 RNAi caused severe delays in mitotic progression, which were substantially rescued by both phosphomimetic and phosphomutant Nde1. Expression of a dynein-binding-deficient Nde1 mutant reduced kinetochore dynein by half, indicating a major role for Nde1 in kinetochore dynein recruitment. These results establish CENP-F as the first well-characterized Nde1 cargo protein, and reveal phosphorylation control of Nde1 cargo binding throughout a substantial fraction of the cell cycle.
MeSH term(s)	Anaphase/physiology ; CDC2 Protein Kinase/metabolism ; Carrier Proteins/metabolism ; Cell Line, Tumor ; Chromosomal Proteins, Non-Histone/metabolism ; Cytoplasmic Dyneins/metabolism ; G2 Phase/physiology ; HeLa Cells ; Humans ; Kinetochores/metabolism ; Microfilament Proteins/metabolism ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Mitosis/genetics ; Nuclear Envelope/metabolism ; Phosphorylation ; Protein Binding ; RNA Interference ; RNA, Small Interfering/genetics
Chemical Substances	Carrier Proteins ; Chromosomal Proteins, Non-Histone ; Microfilament Proteins ; Microtubule-Associated Proteins ; NDEL1 protein, human ; Nde1 protein, human ; RNA, Small Interfering ; centromere protein F ; CDC2 Protein Kinase (EC 2.7.11.22) ; CDK1 protein, human (EC 2.7.11.22) ; Cytoplasmic Dyneins (EC 3.6.4.2)
Language	English
Publishing date	2018-06-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201707081
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Article ; Online: Roles of the multivalent dynein adaptors BicD2 and RILP in neurons.

Vallee, Richard B / Yi, Julie / Quintremil, Sebastian / Khobrekar, Noopur

Neuroscience letters

2021 Volume 752, Page(s) 135796

Abstract: Cytoplasmic dynein is responsible for all forms of retrograde transport in neurons and other cells. Work over several years has led to the identification of a class of coiled-coil domain containing "adaptor" proteins that are responsible for expanding ... ...

Abstract	Cytoplasmic dynein is responsible for all forms of retrograde transport in neurons and other cells. Work over several years has led to the identification of a class of coiled-coil domain containing "adaptor" proteins that are responsible for expanding dynein's range of cargo interactions, as well as regulating dynein motor behavior. This brief review focuses first on the BicD family of adaptor proteins, which clearly serve to expand the number of dynein cargo interactions. RILP, another adaptor protein, also interacts with multiple proteins. Surprisingly, this is to mediate a series of steps within a common pathway, higher eukaryotic autophagy. These distinct features have important implications for understanding the full range of dynein adaptor functions.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Autophagy ; Humans ; Microfilament Proteins/metabolism ; Microtubule-Associated Proteins/metabolism ; Molecular Chaperones/metabolism ; Nerve Tissue Proteins/metabolism ; Neurons/metabolism ; Nuclear Pore Complex Proteins/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; BICD2 protein, human ; Microfilament Proteins ; Microtubule-Associated Proteins ; Molecular Chaperones ; Nerve Tissue Proteins ; Nuclear Pore Complex Proteins ; RILP protein, human ; SYNE2 protein, human ; ran-binding protein 2
Language	English
Publishing date	2021-03-02
Publishing country	Ireland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	194929-9
ISSN	1872-7972 ; 0304-3940
ISSN (online)	1872-7972
ISSN	0304-3940
DOI	10.1016/j.neulet.2021.135796
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Article ; Online: Role of cytoplasmic dynein and kinesins in adenovirus transport.

Scherer, Julian / Yi, Julie / Vallee, Richard B

FEBS letters

2020 Volume 594, Issue 12, Page(s) 1838–1847

Abstract: Following receptor-mediated uptake into endocytic vesicles and subsequent escape, adenovirus particles are transported along microtubules. The microtubule motor proteins dynein and one or more kinesins are involved in this behavior. Dynein is implicated ... ...

Abstract	Following receptor-mediated uptake into endocytic vesicles and subsequent escape, adenovirus particles are transported along microtubules. The microtubule motor proteins dynein and one or more kinesins are involved in this behavior. Dynein is implicated in adenovirus transport toward the nucleus. The kinesin Kif5B has now been found to move the adenovirus (AdV) toward microtubule plus ends, though a kinesin role in adenovirus-induced nuclear pore disruption has also been reported. In undifferentiated cells, dynein-mediated transport predominates early in infection, but motility becomes bidirectional with time. The latter behavior can be modeled as a novel assisted diffusion mechanism, which may allow virus particles to explore the cytoplasm more efficiently. Cytoplasmic dynein and Kif5B have both been found to bind AdV through direct interactions with the capsid proteins hexon and penton base, respectively. We review here the roles of the microtubule motor proteins in AdV infection, the relationship between motor protein recruitment to pathogenic vs. physiological cargoes, the evolutionary origins of microtubule-mediated AdV transport, and a role for the motor proteins in a novel host-defense mechanism.
MeSH term(s)	Adenoviridae/metabolism ; Adenoviridae/pathogenicity ; Adenoviridae Infections/metabolism ; Adenoviridae Infections/virology ; Animals ; Biological Transport ; Capsid Proteins/metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Cytoplasmic Dyneins/metabolism ; Host-Pathogen Interactions/physiology ; Humans ; Kinesin/metabolism ; Virus Internalization
Chemical Substances	Capsid Proteins ; hexon capsid protein, Adenovirus ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11) ; Cytoplasmic Dyneins (EC 3.6.4.2) ; Kinesin (EC 3.6.4.4)
Language	English
Publishing date	2020-04-13
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1002/1873-3468.13777
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Book: Molecular motors and the cytoskeleton / [A]

Vallee, Richard B.

(Methods in enzymology ; 196)

1991

Author's details	ed. by Richard B. Vallee
Series title	Methods in enzymology ; 196 Molecular motors and the cytoskeleton
Collection	Molecular motors and the cytoskeleton
Keywords	Zellskelett ; Motilität ; Molekularbiologie
Subject	Molekulare Biologie ; Bewegungsfähigkeit ; Beweglichkeit ; Motility ; Cytoskelett ; Zytoskelett
Language	English
Size	XXX, 559 S. : Ill., graph. Darst.
Publisher	Academic Press
Publishing place	San Diego u.a.
Publishing country	United States
Document type	Book
HBZ-ID	HT003788720
ISBN	0-12-182097-1 ; 978-0-12-182097-8
Database	Catalogue ZB MED Medicine, Health

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Se 222 -196-	verfügbar in Königswinter	Königswinter

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Book: Molecular motors and the cytoskeleton / [A]

Vallee, Richard B.

(Methods in enzymology ; 196)

1991

Author's details	ed. by Richard B. Vallee
Series title	Methods in enzymology ; 196 Molecular motors and the cytoskeleton
Collection	Molecular motors and the cytoskeleton
Keywords	Zellskelett ; Motilität ; Molekularbiologie
Subject	Molekulare Biologie ; Bewegungsfähigkeit ; Beweglichkeit ; Motility ; Cytoskelett ; Zytoskelett
Language	English
Size	XXX, 559 S. : Ill., graph. Darst.
Publisher	Academic Press
Publishing place	San Diego u.a.
Publishing country	United States
Document type	Book
HBZ-ID	HT003788720
ISBN	0-12-182097-1 ; 978-0-12-182097-8
Database	Catalogue ZB MED Nutrition, Environment, Agriculture

In stock of ZB MED Bonn / Germany

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918/1869	available for loan (reading room)	Freihandmagazin (U1)

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