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Article ; Online: The E3 ligase Poe promotes Pericentrin degradation.

Galletta, Brian J / Varadarajan, Ramya / Fagerstrom, Carey J / Yang, Bing / Haase, Karen Plevock / McJunkin, Katherine / Rusan, Nasser M

Molecular biology of the cell

2023 Volume 34, Issue 9, Page(s) br15

Abstract: Centrosomes are essential parts of diverse cellular processes, and precise regulation of the levels of their constituent proteins is critical for their function. One such protein is Pericentrin (PCNT) in humans and Pericentrin-like protein (PLP) ... ...

Abstract	Centrosomes are essential parts of diverse cellular processes, and precise regulation of the levels of their constituent proteins is critical for their function. One such protein is Pericentrin (PCNT) in humans and Pericentrin-like protein (PLP) in
MeSH term(s)	Male ; Humans ; Ubiquitin-Protein Ligases/metabolism ; Centrioles/metabolism ; Centrosome/metabolism ; Antigens/metabolism
Chemical Substances	Ubiquitin-Protein Ligases (EC 2.3.2.27) ; pericentrin ; Antigens
Language	English
Publishing date	2023-06-21
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.E22-11-0534
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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: Spd-2 gene duplication reveals cell-type-specific pericentriolar material regulation.

O'Neill, Ryan S / Sodeinde, Afeez K / Welsh, Frances C / Fagerstrom, Carey J / Galletta, Brian J / Rusan, Nasser M

Current biology : CB

2023 Volume 33, Issue 14, Page(s) 3031–3040.e6

Abstract: Centrosomes are multi-protein organelles that function as microtubule (MT) organizing centers (MTOCs), ensuring spindle formation and chromosome segregation during cell division. ...

Abstract	Centrosomes are multi-protein organelles that function as microtubule (MT) organizing centers (MTOCs), ensuring spindle formation and chromosome segregation during cell division.
MeSH term(s)	Animals ; Male ; Centrioles/genetics ; Centrioles/metabolism ; Centrosome/metabolism ; Drosophila/genetics ; Drosophila/metabolism ; Gene Duplication ; Meiosis ; Mitosis ; Tubulin/metabolism ; Cytoskeletal Proteins/genetics ; Drosophila Proteins/genetics
Chemical Substances	Tubulin ; SPD-2 protein, Drosophila ; Cytoskeletal Proteins ; Drosophila Proteins
Language	English
Publishing date	2023-06-27
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2023.06.020
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Article ; Online: Cep104 is a component of the centriole distal tip complex that regulates centriole growth and contributes to Drosophila spermiogenesis.

Ryniawec, John M / Hannaford, Matthew R / Zibrat, Melanie E / Fagerstrom, Carey J / Galletta, Brian J / Aguirre, Sophia E / Guice, Bethany A / Dean, Spencer M / Rusan, Nasser M / Rogers, Gregory C

Current biology : CB

2023 Volume 33, Issue 19, Page(s) 4202–4216.e9

Abstract: Proper centrosome number and function relies on the accurate assembly of centrioles, barrel-shaped structures that form the core duplicating elements of the organelle. The growth of centrioles is regulated in a cell cycle-dependent manner; while new ... ...

Abstract	Proper centrosome number and function relies on the accurate assembly of centrioles, barrel-shaped structures that form the core duplicating elements of the organelle. The growth of centrioles is regulated in a cell cycle-dependent manner; while new daughter centrioles elongate during the S/G2/M phase, mature mother centrioles maintain their length throughout the cell cycle. Centriole length is controlled by the synchronized growth of the microtubules that ensheathe the centriole barrel. Although proteins exist that target the growing distal tips of centrioles, such as CP110 and Cep97, these proteins are generally thought to suppress centriolar microtubule growth, suggesting that distal tips may also contain unidentified counteracting factors that facilitate microtubule polymerization. Currently, a mechanistic understanding of how distal tip proteins balance microtubule growth and shrinkage to either promote daughter centriole elongation or maintain centriole length is lacking. Using a proximity-labeling screen in Drosophila cells, we identified Cep104 as a novel component of a group of evolutionarily conserved proteins that we collectively refer to as the distal tip complex (DTC). We found that Cep104 regulates centriole growth and promotes centriole elongation through its microtubule-binding TOG domain. Furthermore, analysis of Cep104 null flies revealed that Cep104 and Cep97 cooperate during spermiogenesis to align spermatids and coordinate individualization. Lastly, we mapped the complete DTC interactome and showed that Cep97 is the central scaffolding unit required to recruit DTC components to the distal tip of centrioles.
MeSH term(s)	Male ; Animals ; Centrioles/metabolism ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Drosophila/metabolism ; Centrosome/metabolism ; Spermatogenesis ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism
Chemical Substances	Microtubule-Associated Proteins ; Cell Cycle Proteins
Language	English
Publishing date	2023-09-19
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, N.I.H., Extramural
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2023.08.075
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Article: A yeast two-hybrid approach for probing protein-protein interactions at the centrosome.

Galletta, Brian J / Rusan, Nasser M

Methods in cell biology

2015 Volume 129, Page(s) 251–277

Abstract: As a large, nonmembrane bound organelle, the centrosome must rely heavily on protein-protein interactions to assemble itself in the cytoplasm and perform its functions as a microtubule-organizing center. Therefore, to understand how this organelle is ... ...

Abstract	As a large, nonmembrane bound organelle, the centrosome must rely heavily on protein-protein interactions to assemble itself in the cytoplasm and perform its functions as a microtubule-organizing center. Therefore, to understand how this organelle is built and functions, one must understand the protein-protein interactions made by each centrosome protein. Unfortunately, the highly interconnected nature of the centrosome, combined with its predicted unstructured, coil-rich proteins, has made the use of many standard approaches to studying protein-protein interactions very challenging. The yeast-two hybrid (Y2H) system is well suited for studying the centrosome and is an important complement to other biochemical approaches. In this chapter we describe how to carry out a directed Y2H screen to identify the direct interactions between a given centrosome protein and a library of others. Specifically, we detail using a bioinformatics-based approach (structure prediction programs) to subdivide proteins and screen for interactions using an array-based Y2H approach. We also describe how to use the interaction information garnered from this screen to generate mutations to disrupt specific interactions using mutagenic-PCR and a "reverse" Y2H screen. Finally, we discuss how information from such a screen can be integrated into existing models of centrosome assembly and how it can initiate and guide extensive in vitro and in vivo experimentation to test these models.
MeSH term(s)	Centrosome/physiology ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins/physiology ; Two-Hybrid System Techniques
Chemical Substances	Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2015-05-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ISSN	0091-679X
ISSN	0091-679X
DOI	10.1016/bs.mcb.2015.03.012
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Article ; Online: Sperm Head-Tail Linkage Requires Restriction of Pericentriolar Material to the Proximal Centriole End.

Galletta, Brian J / Ortega, Jacob M / Smith, Samantha L / Fagerstrom, Carey J / Fear, Justin M / Mahadevaraju, Sharvani / Oliver, Brian / Rusan, Nasser M

Developmental cell

2020 Volume 53, Issue 1, Page(s) 86–101.e7

Abstract: The centriole, or basal body, is the center of attachment between the sperm head and tail. While the distal end of the centriole templates the cilia, the proximal end associates with the nucleus. Using Drosophila, we identify a centriole-centric ... ...

Abstract	The centriole, or basal body, is the center of attachment between the sperm head and tail. While the distal end of the centriole templates the cilia, the proximal end associates with the nucleus. Using Drosophila, we identify a centriole-centric mechanism that ensures proper proximal end docking to the nucleus. This mechanism relies on the restriction of pericentrin-like protein (PLP) and the pericentriolar material (PCM) to the proximal end of the centriole. PLP is restricted proximally by limiting its mRNA and protein to the earliest stages of centriole elongation. Ectopic positioning of PLP to more distal portions of the centriole is sufficient to redistribute PCM and microtubules along the entire centriole length. This results in erroneous, lateral centriole docking to the nucleus, leading to spermatid decapitation as a result of a failure to form a stable head-tail linkage.
MeSH term(s)	Animals ; Basal Bodies/metabolism ; Centrioles/metabolism ; Centrosome/metabolism ; Drosophila Proteins/metabolism ; Drosophila melanogaster/metabolism ; Male ; Microtubules/metabolism ; Sperm Head/metabolism ; Sperm Tail/metabolism
Chemical Substances	Drosophila Proteins
Language	English
Publishing date	2020-03-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2020.02.006
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Zs.A 5742: 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)
Zs.MG 76: Show issues

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Article ; Online: Pericentrin interacts with Kinesin-1 to drive centriole motility.

Hannaford, Matthew R / Liu, Rong / Billington, Neil / Swider, Zachary T / Galletta, Brian J / Fagerstrom, Carey J / Combs, Christian / Sellers, James R / Rusan, Nasser M

The Journal of cell biology

2022 Volume 221, Issue 9

Abstract: Centrosome positioning is essential for their function. Typically, centrosomes are transported to various cellular locations through the interaction of centrosomal microtubules (MTs) with motor proteins anchored at the cortex or the nuclear surface. ... ...

Abstract	Centrosome positioning is essential for their function. Typically, centrosomes are transported to various cellular locations through the interaction of centrosomal microtubules (MTs) with motor proteins anchored at the cortex or the nuclear surface. However, it remains unknown how centrioles migrate in cellular contexts in which they do not nucleate MTs. Here, we demonstrate that during interphase, inactive centrioles move directly along the interphase MT network as Kinesin-1 cargo. We identify Pericentrin-Like-Protein (PLP) as a novel Kinesin-1 interacting molecule essential for centriole motility. In vitro assays show that PLP directly interacts with the cargo binding domain of Kinesin-1, allowing PLP to migrate on MTs. Binding assays using purified proteins revealed that relief of Kinesin-1 autoinhibition is critical for its interaction with PLP. Finally, our studies of neural stem cell asymmetric divisions in the Drosophila brain show that the PLP-Kinesin-1 interaction is essential for the timely separation of centrioles, the asymmetry of centrosome activity, and the age-dependent centrosome inheritance.
MeSH term(s)	Animals ; Antigens/metabolism ; Calmodulin-Binding Proteins/metabolism ; Centrioles/metabolism ; Centrosome/metabolism ; Drosophila ; Drosophila Proteins/metabolism ; Kinesins/metabolism ; Microtubules/metabolism ; Neural Stem Cells ; Protein Transport
Chemical Substances	Antigens ; Calmodulin-Binding Proteins ; Drosophila Proteins ; Plp protein, Drosophila ; pericentrin ; Khc protein, Drosophila (EC 3.6.1.-) ; Kinesins (EC 3.6.4.4)
Language	English
Publishing date	2022-08-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202112097
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Article ; Online: Asterless is required for centriole length control and sperm development.

Galletta, Brian J / Jacobs, Katherine C / Fagerstrom, Carey J / Rusan, Nasser M

The Journal of cell biology

2016 Volume 213, Issue 4, Page(s) 435–450

Abstract: Centrioles are the foundation of two organelles, centrosomes and cilia. Centriole numbers and functions are tightly controlled, and mutations in centriole proteins are linked to a variety of diseases, including microcephaly. Loss of the centriole protein ...

Abstract	Centrioles are the foundation of two organelles, centrosomes and cilia. Centriole numbers and functions are tightly controlled, and mutations in centriole proteins are linked to a variety of diseases, including microcephaly. Loss of the centriole protein Asterless (Asl), the Drosophila melanogaster orthologue of Cep152, prevents centriole duplication, which has limited the study of its nonduplication functions. Here, we identify populations of cells with Asl-free centrioles in developing Drosophila tissues, allowing us to assess its duplication-independent function. We show a role for Asl in controlling centriole length in germline and somatic tissue, functioning via the centriole protein Cep97. We also find that Asl is not essential for pericentriolar material recruitment or centrosome function in organizing mitotic spindles. Lastly, we show that Asl is required for proper basal body function and spermatid axoneme formation. Insights into the role of Asl/Cep152 beyond centriole duplication could help shed light on how Cep152 mutations lead to the development of microcephaly.
MeSH term(s)	Animals ; Axoneme/metabolism ; Axoneme/physiology ; Basal Bodies/metabolism ; Basal Bodies/physiology ; Cell Cycle Proteins/metabolism ; Centrioles/metabolism ; Centrioles/physiology ; Drosophila Proteins/metabolism ; Drosophila melanogaster/metabolism ; Drosophila melanogaster/physiology ; Male ; Mitosis/physiology ; Spermatozoa/growth & development ; Spermatozoa/metabolism ; Spermatozoa/physiology
Chemical Substances	Asl protein, Drosophila ; Cell Cycle Proteins ; Drosophila Proteins
Language	English
Publishing date	2016-05-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201501120
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Article ; Online: Actin-Regulator Feedback Interactions during Endocytosis.

Wang, Xinxin / Galletta, Brian J / Cooper, John A / Carlsson, Anders E

Biophysical journal

2016 Volume 110, Issue 6, Page(s) 1430–1443

Abstract: Endocytosis mediated by clathrin, a cellular process by which cells internalize membrane receptors and their extracellular ligands, is an important component of cell signaling regulation. Actin polymerization is involved in endocytosis in varying degrees ...

Abstract	Endocytosis mediated by clathrin, a cellular process by which cells internalize membrane receptors and their extracellular ligands, is an important component of cell signaling regulation. Actin polymerization is involved in endocytosis in varying degrees depending on the cellular context. In yeast, clathrin-mediated endocytosis requires a pulse of polymerized actin and its regulators, which recruit and activate the Arp2/3 complex. In this article, we seek to identify the main protein-protein interactions that 1) cause actin and its regulators to appear in pulses, and 2) determine the effects of key mutations and drug treatments on actin and regulator assembly. We perform a joint modeling/experimental study of actin and regulator dynamics during endocytosis in the budding yeast Saccharomyces cerevisiae. We treat both a stochastic model that grows an explicit three-dimensional actin network, and a simpler two-variable Fitzhugh-Nagumo type model. The models include a negative-feedback interaction of F-actin onto the Arp2/3 regulators. Both models explain the pulse time courses and the effects of interventions on actin polymerization: the surprising increase in the peak F-actin count caused by reduced regulator branching activity, the increase in F-actin resulting from slowing of actin disassembly, and the increased Arp2/3 regulator lifetime resulting from latrunculin treatment. In addition, they predict that decreases in the regulator branching activity lead to increases in accumulation of regulators, and we confirmed this prediction with experiments on yeast harboring mutations in the Arp2/3 regulators, using quantitative fluorescence microscopy. Our experimental measurements suggest that the regulators act quasi-independently, in the sense that accumulation of a particular regulator is most strongly affected by mutations of that regulator, as opposed to the others.
MeSH term(s)	Actins/metabolism ; Computer Simulation ; Endocytosis ; Feedback, Physiological ; Models, Biological ; Mutation/genetics ; Protein Domains ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Stochastic Processes ; Time Factors
Chemical Substances	Actins ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2016-03-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	218078-9
ISSN	1542-0086 ; 0006-3495
ISSN (online)	1542-0086
ISSN	0006-3495
DOI	10.1016/j.bpj.2016.02.018
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Zs.A 235: 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 2: Show issues

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Article ; Online: Actin and endocytosis: mechanisms and phylogeny.

Galletta, Brian J / Cooper, John A

Current opinion in cell biology

2009 Volume 21, Issue 1, Page(s) 20–27

Abstract: The regulated assembly of actin filament networks is a crucial part of endocytosis, with crucial temporal and spatial relationships between proteins of the endocytic and actin assembly machinery. Of particular importance has been a wealth of studies in ... ...

Abstract	The regulated assembly of actin filament networks is a crucial part of endocytosis, with crucial temporal and spatial relationships between proteins of the endocytic and actin assembly machinery. Of particular importance has been a wealth of studies in budding and fission yeast. Cell biology approaches, combined with molecular genetics, have begun to uncover the complexity of the regulation of actin dynamics during the endocytic process. In a wide range of organisms, clathrin-mediated endocytosis appears to be linked to Arp2/3-mediated actin assembly. The conservation of the components, across a wide range eukaryotic species, suggests that the partnership between endocytosis and actin may be evolutionarily ancient.
MeSH term(s)	Actins/genetics ; Actins/metabolism ; Animals ; Biological Evolution ; Endocytosis ; Eukaryotic Cells/metabolism ; Phylogeny
Chemical Substances	Actins
Language	English
Publishing date	2009-01-29
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1026381-0
ISSN	1879-0410 ; 0955-0674
ISSN (online)	1879-0410
ISSN	0955-0674
DOI	10.1016/j.ceb.2009.01.006
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Zs.A 2963: Show issues

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Article ; Online: Newly Characterized Region of CP190 Associates with Microtubules and Mediates Proper Spindle Morphology in Drosophila Stem Cells.

Plevock, Karen M / Galletta, Brian J / Slep, Kevin C / Rusan, Nasser M

PloS one

2015 Volume 10, Issue 12, Page(s) e0144174

Abstract: CP190 is a large, multi-domain protein, first identified as a centrosome protein with oscillatory localization over the course of the cell cycle. During interphase it has a well-established role within the nucleus as a chromatin insulator. Upon nuclear ... ...

Abstract	CP190 is a large, multi-domain protein, first identified as a centrosome protein with oscillatory localization over the course of the cell cycle. During interphase it has a well-established role within the nucleus as a chromatin insulator. Upon nuclear envelope breakdown, there is a striking redistribution of CP190 to centrosomes and the mitotic spindle, in addition to the population at chromosomes. Here, we investigate CP190 in detail by performing domain analysis in cultured Drosophila S2 cells combined with protein structure determination by X-ray crystallography, in vitro biochemical characterization, and in vivo fixed and live imaging of cp190 mutant flies. Our analysis of CP190 identifies a novel N-terminal centrosome and microtubule (MT) targeting region, sufficient for spindle localization. This region consists of a highly conserved BTB domain and a linker region that serves as the MT binding domain. We present the 2.5 Å resolution structure of the CP190 N-terminal 126 amino acids, which adopts a canonical BTB domain fold and exists as a stable dimer in solution. The ability of the linker region to robustly localize to MTs requires BTB domain-mediated dimerization. Deletion of the linker region using CRISPR significantly alters spindle morphology and leads to DNA segregation errors in the developing Drosophila brain neuroblasts. Collectively, we highlight a multivalent MT-binding architecture in CP190, which confers distinct subcellular cytoskeletal localization and function during mitosis.
MeSH term(s)	Animals ; Cell Nucleus ; Centrosome ; Chromosome Segregation ; Chromosomes ; Clustered Regularly Interspaced Short Palindromic Repeats ; Crystallography, X-Ray ; DNA/metabolism ; Drosophila Proteins/physiology ; Drosophila melanogaster/genetics ; Microtubule-Associated Proteins/physiology ; Microtubules/metabolism ; Mitosis/physiology ; Nuclear Proteins/physiology ; Spindle Apparatus/metabolism ; Spindle Apparatus/ultrastructure ; Stem Cells/metabolism
Chemical Substances	CP190 protein, Drosophila ; Drosophila Proteins ; Microtubule-Associated Proteins ; Nuclear Proteins ; DNA (9007-49-2)
Language	English
Publishing date	2015-12-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0144174
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