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Article ; Online: BORG family proteins in physiology and human disease.

Tomasso, Meagan R / Padrick, Shae B

2023 Volume 80, Issue 7-8, Page(s) 182–198

Abstract: The binder of rho GTPases (BORG)/Cdc42 effector proteins (Cdc42EP) family is composed of five Rho GTPase binding proteins whose functions and mechanism of actions are of emerging interest. Here, we review recent findings pertaining to the family as a ... ...

Abstract	The binder of rho GTPases (BORG)/Cdc42 effector proteins (Cdc42EP) family is composed of five Rho GTPase binding proteins whose functions and mechanism of actions are of emerging interest. Here, we review recent findings pertaining to the family as a whole and consider how these change our understanding of cellular organization. Recent studies have implicated BORGs in both fundamental physiology and in human diseases, mainly cancers. An emerging pattern suggests that BORG family members cancer-promoting properties are related to their ability to regulate the cytoskeleton, with many impacting the organization of acto-myosin stress fibers. This is consistent with the broader literature indicating that BORG family members are regulators of both the septin and actin cytoskeleton networks. The exact mechanism through which BORGs modify the cytoskeleton is not clear, but we consider here a few data-supported and speculative possibilities. Finally, we delve into how the Rho GTPase Cdc42 modifies BORG function in cells. This remains open-ended as Cdc42's effects on BORGs appear cell type- and cell state-dependent. Collectively, these data point to the importance of the BORG family and suggest broader themes in their function and regulation.
MeSH term(s)	Humans ; rho GTP-Binding Proteins/metabolism ; cdc42 GTP-Binding Protein/metabolism ; Cytoskeleton/metabolism ; Actin Cytoskeleton/metabolism ; Microtubules/metabolism ; Septins/metabolism
Chemical Substances	rho GTP-Binding Proteins (EC 3.6.5.2) ; cdc42 GTP-Binding Protein (EC 3.6.5.2) ; Septins (EC 3.6.1.-)
Language	English
Publishing date	2023-07-05
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2534372-5
ISSN	1949-3592 ; 1949-3584
ISSN (online)	1949-3592
ISSN	1949-3584
DOI	10.1002/cm.21768
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Article ; Online: Cyclase-associated protein interacts with actin filament barbed ends to promote depolymerization and formin displacement.

Alimov, Nikita / Hoeprich, Gregory J / Padrick, Shae B / Goode, Bruce L

The Journal of biological chemistry

2023 Volume 299, Issue 12, Page(s) 105367

Abstract: Cyclase-associated protein (CAP) has emerged as a central player in cellular actin turnover, but its molecular mechanisms of action are not yet fully understood. Recent studies revealed that the N terminus of CAP interacts with the pointed ends of actin ... ...

Abstract	Cyclase-associated protein (CAP) has emerged as a central player in cellular actin turnover, but its molecular mechanisms of action are not yet fully understood. Recent studies revealed that the N terminus of CAP interacts with the pointed ends of actin filaments to accelerate depolymerization in conjunction with cofilin. Here, we use in vitro microfluidics-assisted TIRF microscopy to show that the C terminus of CAP promotes depolymerization at the opposite (barbed) ends of actin filaments. In the absence of actin monomers, full-length mouse CAP1 and C-terminal halves of CAP1 (C-CAP1) and CAP2 (C-CAP2) accelerate barbed end depolymerization. Using mutagenesis and structural modeling, we show that these activities are mediated by the WH2 and CARP domains of CAP. In addition, we observe that CAP collaborates with profilin to accelerate barbed end depolymerization and that these effects depend on their direct interaction, providing the first known example of CAP-profilin collaborative effects in regulating actin. In the presence of actin monomers, CAP1 attenuates barbed end growth and promotes formin dissociation. Overall, these findings demonstrate that CAP uses distinct domains and mechanisms to interact with opposite ends of actin filaments and drive turnover. Further, they contribute to the emerging view of actin barbed ends as sites of dynamic molecular regulation, where numerous proteins compete and cooperate with each other to tune polymer dynamics, similar to the rich complexity seen at microtubule ends.
MeSH term(s)	Animals ; Mice ; Actin Cytoskeleton/chemistry ; Actin Cytoskeleton/metabolism ; Actin Depolymerizing Factors/genetics ; Actin Depolymerizing Factors/metabolism ; Actins/chemistry ; Actins/metabolism ; Formins/metabolism ; Profilins/metabolism ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Polymerization ; Protein Domains/genetics ; Models, Molecular ; Protein Structure, Tertiary
Chemical Substances	Actin Depolymerizing Factors ; Actins ; Formins ; Profilins ; Cytoskeletal Proteins ; Membrane Proteins
Language	English
Publishing date	2023-10-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.105367
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Article ; Online: Direct observation of cortactin protecting Arp2/3-actin filament branch junctions from GMF-mediated destabilization.

McGuirk, Emma R / Koundinya, Neha / Nagarajan, Priyashree / Padrick, Shae B / Goode, Bruce L

European journal of cell biology

2023 Volume 103, Issue 1, Page(s) 151378

Abstract: How cells tightly control the formation and turnover of branched actin filament arrays to drive cell motility, endocytosis, and other cellular processes is still not well understood. Here, we investigated the mechanistic relationship between two binding ... ...

Abstract	How cells tightly control the formation and turnover of branched actin filament arrays to drive cell motility, endocytosis, and other cellular processes is still not well understood. Here, we investigated the mechanistic relationship between two binding partners of the Arp2/3 complex, glia maturation factor (GMF) and cortactin. Individually, GMF and cortactin have opposite effects on the stability of actin filament branches, but it is unknown how they work in concert with each other to govern branch turnover. Using TIRF microscopy, we observe that GMF's branch destabilizing activities are potently blocked by cortactin (IC
MeSH term(s)	Glia Maturation Factor/genetics ; Glia Maturation Factor/chemistry ; Glia Maturation Factor/metabolism ; Cortactin ; Actins/metabolism ; Actin Cytoskeleton/metabolism ; Actin-Related Protein 2-3 Complex/metabolism
Chemical Substances	Glia Maturation Factor ; Cortactin ; Actins ; Actin-Related Protein 2-3 Complex
Language	English
Publishing date	2023-12-05
Publishing country	Germany
Document type	Journal Article
ZDB-ID	391967-5
ISSN	1618-1298 ; 0070-2463 ; 0171-9335
ISSN (online)	1618-1298
ISSN	0070-2463 ; 0171-9335
DOI	10.1016/j.ejcb.2023.151378
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Article ; Online: Structure of VanS from vancomycin-resistant enterococci: A sensor kinase with weak ATP binding.

Grasty, Kimberly C / Guzik, Claudia / D'Lauro, Elizabeth J / Padrick, Shae B / Beld, Joris / Loll, Patrick J

The Journal of biological chemistry

2023 Volume 299, Issue 3, Page(s) 103001

Abstract: The VanRS two-component system regulates the resistance phenotype of vancomycin-resistant enterococci. VanS is a sensor histidine kinase that responds to the presence of vancomycin by autophosphorylating and subsequently transferring the phosphoryl group ...

Abstract	The VanRS two-component system regulates the resistance phenotype of vancomycin-resistant enterococci. VanS is a sensor histidine kinase that responds to the presence of vancomycin by autophosphorylating and subsequently transferring the phosphoryl group to the response regulator, VanR. The phosphotransfer activates VanR as a transcription factor, which initiates the expression of resistance genes. Structural information about VanS proteins has remained elusive, hindering the molecular-level understanding of their function. Here, we present X-ray crystal structures for the catalytic and ATP-binding (CA) domains of two VanS proteins, derived from vancomycin-resistant enterococci types A and C. Both proteins adopt the canonical Bergerat fold that has been observed for CA domains of other prokaryotic histidine kinases. We attempted to determine structures for the nucleotide-bound forms of both proteins; however, despite repeated efforts, these forms could not be crystallized, prompting us to measure the proteins' binding affinities for ATP. Unexpectedly, both CA domains displayed low affinities for the nucleotide, with K
MeSH term(s)	Vancomycin-Resistant Enterococci/metabolism ; Protein Kinases/genetics ; Protein Kinases/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Transcription Factors/metabolism ; Histidine Kinase/genetics ; Histidine Kinase/metabolism ; Nucleotides ; Adenosine Triphosphate ; Anti-Bacterial Agents/metabolism
Chemical Substances	Protein Kinases (EC 2.7.-) ; Bacterial Proteins ; Transcription Factors ; Histidine Kinase (EC 2.7.13.1) ; Nucleotides ; Adenosine Triphosphate (8L70Q75FXE) ; Anti-Bacterial Agents
Language	English
Publishing date	2023-02-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.103001
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Article ; Online: Septins mediate a microtubule-actin crosstalk that enables actin growth on microtubules.

Nakos, Konstantinos / Alam, Md Noor A / Radler, Megan R / Kesisova, Ilona A / Yang, Changsong / Okletey, Joshua / Tomasso, Meagan R / Padrick, Shae B / Svitkina, Tatyana M / Spiliotis, Elias T

Proceedings of the National Academy of Sciences of the United States of America

2022 Volume 119, Issue 50, Page(s) e2202803119

Abstract: Cellular morphogenesis and processes such as cell division and migration require the coordination of the microtubule and actin cytoskeletons. Microtubule-actin crosstalk is poorly understood and largely regarded as the capture and regulation of ... ...

Abstract	Cellular morphogenesis and processes such as cell division and migration require the coordination of the microtubule and actin cytoskeletons. Microtubule-actin crosstalk is poorly understood and largely regarded as the capture and regulation of microtubules by actin. Septins are filamentous guanosine-5'-triphosphate (GTP) binding proteins, which comprise the fourth component of the cytoskeleton along microtubules, actin, and intermediate filaments. Here, we report that septins mediate microtubule-actin crosstalk by coupling actin polymerization to microtubule lattices. Superresolution and platinum replica electron microscopy (PREM) show that septins localize to overlapping microtubules and actin filaments in the growth cones of neurons and non-neuronal cells. We demonstrate that recombinant septin complexes directly crosslink microtubules and actin filaments into hybrid bundles. In vitro reconstitution assays reveal that microtubule-bound septins capture and align stable actin filaments with microtubules. Strikingly, septins enable the capture and polymerization of growing actin filaments on microtubule lattices. In neuronal growth cones, septins are required for the maintenance of the peripheral actin network that fans out from microtubules. These findings show that septins directly mediate microtubule interactions with actin filaments, and reveal a mechanism of microtubule-templated actin growth with broader significance for the self-organization of the cytoskeleton and cellular morphogenesis.
MeSH term(s)	Septins ; Actins ; Microtubules
Chemical Substances	Septins (EC 3.6.1.-) ; Actins
Language	English
Publishing date	2022-12-07
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2202803119
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Article ; Online: Production and analysis of a mammalian septin hetero-octamer complex.

DeRose, Barry T / Kelley, Robert S / Ravi, Roshni / Kokona, Bashkim / Beld, Joris / Spiliotis, Elias T / Padrick, Shae B

Cytoskeleton (Hoboken, N.J.)

2020 Volume 77, Issue 11, Page(s) 485–499

Abstract: The septins are filament-forming proteins found in diverse eukaryotes from fungi to vertebrates, with roles in cytokinesis, shaping of membranes and modifying cytoskeletal organization. These GTPases assemble into rod-shaped soluble hetero-hexamers and ... ...

Abstract	The septins are filament-forming proteins found in diverse eukaryotes from fungi to vertebrates, with roles in cytokinesis, shaping of membranes and modifying cytoskeletal organization. These GTPases assemble into rod-shaped soluble hetero-hexamers and hetero-octamers in mammals, which polymerize into filaments and higher order structures. While the cell biology and pathobiology of septins are advancing rapidly, mechanistic study of the mammalian septins is limited by a lack of recombinant hetero-octamer materials. We describe here the production and characterization of a recombinant mammalian septin hetero-octamer of defined stoichiometry, the SEPT2/SEPT6/SEPT7/SEPT3 complex. Using a fluorescent protein fusion to the complex, we observed filaments assembled from this complex. In addition, we used this novel tool to resolve recent questions regarding the organization of the soluble septin complex. Biochemical characterization of a SEPT3 truncation that disrupts SEPT3-SEPT3 interactions is consistent with SEPT3 occupying a central position in the complex while the SEPT2 subunits are at the ends of the rod-shaped octameric complexes. Consistent with SEPT2 being on the complex ends, we find that our purified SEPT2/SEPT6/SEPT7/SEPT3 hetero-octamer copolymerizes into mixed filaments with separately purified SEPT2/SEPT6/SEPT7 hetero-hexamer. We expect this new recombinant production approach to lay essential groundwork for future studies into mammalian septin mechanism and function.
MeSH term(s)	Animals ; Mammals ; Protein Multimerization ; Septins/metabolism
Chemical Substances	Septins (EC 3.6.1.-)
Language	English
Publishing date	2020-11-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2534372-5
ISSN	1949-3592 ; 1949-3584
ISSN (online)	1949-3592
ISSN	1949-3584
DOI	10.1002/cm.21643
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Article ; Online: On the acquisition and analysis of microscale thermophoresis data.

Scheuermann, Thomas H / Padrick, Shae B / Gardner, Kevin H / Brautigam, Chad A

Analytical biochemistry

2016 Volume 496, Page(s) 79–93

Abstract: A comprehensive understanding of the molecular mechanisms underpinning cellular functions is dependent on a detailed characterization of the energetics of macromolecular binding, often quantified by the equilibrium dissociation constant, KD. While many ... ...

Abstract	A comprehensive understanding of the molecular mechanisms underpinning cellular functions is dependent on a detailed characterization of the energetics of macromolecular binding, often quantified by the equilibrium dissociation constant, KD. While many biophysical methods may be used to obtain KD, the focus of this report is a relatively new method called microscale thermophoresis (MST). In an MST experiment, a capillary tube filled with a solution containing a dye-labeled solute is illuminated with an infrared laser, rapidly creating a temperature gradient. Molecules will migrate along this gradient, causing changes in the observed fluorescence. Because the net migration of the labeled molecules will depend on their liganded state, a binding curve as a function of ligand concentration can be constructed from MST data and analyzed to determine KD. Herein, simulations demonstrate the limits of KD that can be measured in current instrumentation. They also show that binding kinetics is a major concern in planning and executing MST experiments. Additionally, studies of two protein-protein interactions illustrate challenges encountered in acquiring and analyzing MST data. Combined, these approaches indicate a set of best practices for performing and analyzing MST experiments. Software for rigorous data analysis is also introduced.
MeSH term(s)	Calorimetry/methods ; Fluorescence ; Kinetics ; Ligands ; Monte Carlo Method ; Protein Binding ; Proteins/chemistry
Chemical Substances	Ligands ; Proteins
Language	English
Publishing date	2016-03-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1016/j.ab.2015.12.013
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Article ; Online: Evaluating the stoichiometry of macromolecular complexes using multisignal sedimentation velocity.

Padrick, Shae B / Brautigam, Chad A

Methods (San Diego, Calif.)

2011 Volume 54, Issue 1, Page(s) 39–55

Abstract: Gleaning information regarding the molecular physiology of macromolecular complexes requires knowledge of their component stoichiometries. In this work, a relatively new means of analyzing sedimentation velocity (SV) data from the analytical ... ...

Abstract	Gleaning information regarding the molecular physiology of macromolecular complexes requires knowledge of their component stoichiometries. In this work, a relatively new means of analyzing sedimentation velocity (SV) data from the analytical ultracentrifuge is examined in detail. The method depends on collecting concentration profile data simultaneously using multiple signals, like Rayleigh interferometry and UV spectrophotometry. If the cosedimenting components of a complex are spectrally distinguishable, continuous sedimentation-coefficient distributions specific for each component can be calculated to reveal the molar ratio of the complex's components. When combined with the hydrodynamic information available from the SV data, a stoichiometry can be derived. Herein, the spectral properties of sedimenting species are systematically explored to arrive at a predictive test for whether a set of macromolecules can be spectrally resolved in a multisignal SV (MSSV) experiment. Also, a graphical means of experimental design and criteria to judge the success of the spectral discrimination in MSSV are introduced. A detailed example of the analysis of MSSV experiments is offered, and the possibility of deriving equilibrium association constants from MSSV analyses is explored. Finally, successful implementations of MSSV are reviewed.
MeSH term(s)	Actin-Related Protein 2-3 Complex/chemistry ; Actin-Related Protein 2-3 Complex/metabolism ; Computer Simulation ; Glutathione Transferase/chemistry ; Glutathione Transferase/metabolism ; Kinetics ; Multiprotein Complexes/chemistry ; Ultracentrifugation/methods ; Wiskott-Aldrich Syndrome Protein/chemistry ; Wiskott-Aldrich Syndrome Protein/metabolism
Chemical Substances	Actin-Related Protein 2-3 Complex ; Multiprotein Complexes ; Wiskott-Aldrich Syndrome Protein ; Glutathione Transferase (EC 2.5.1.18)
Language	English
Publishing date	2011-01-20
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1066584-5
ISSN	1095-9130 ; 1046-2023
ISSN (online)	1095-9130
ISSN	1046-2023
DOI	10.1016/j.ymeth.2011.01.002
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Article ; Online: Physical mechanisms of signal integration by WASP family proteins.

Padrick, Shae B / Rosen, Michael K

Annual review of biochemistry

2010 Volume 79, Page(s) 707–735

Abstract: The proteins of the Wiskott-Aldrich syndrome protein (WASP) family are activators of the ubiquitous actin nucleation factor, the Arp2/3 complex. WASP family proteins contain a C-terminal VCA domain that binds and activates the Arp2/3 complex in response ... ...

Abstract	The proteins of the Wiskott-Aldrich syndrome protein (WASP) family are activators of the ubiquitous actin nucleation factor, the Arp2/3 complex. WASP family proteins contain a C-terminal VCA domain that binds and activates the Arp2/3 complex in response to numerous inputs, including Rho family GTPases, phosphoinositide lipids, SH3 domain-containing proteins, kinases, and phosphatases. In the archetypal members of the family, WASP and N-WASP, these signals are integrated through two levels of regulation, an allosteric autoinhibitory interaction, in which the VCA is sequestered from the Arp2/3 complex, and dimerization/oligomerization, in which multi-VCA complexes are better activators of the Arp2/3 complex than monomers. Here, we review the structural, biochemical, and biophysical details of these mechanisms and illustrate how they work together to control WASP activity in response to multiple inputs. These regulatory principles, derived from studies of WASP and N-WASP, are likely to apply broadly across the family.
MeSH term(s)	Actin-Related Protein 2-3 Complex/metabolism ; Allosteric Regulation ; Humans ; Protein Multimerization ; Protein Structure, Tertiary ; Signal Transduction ; Wiskott-Aldrich Syndrome Protein Family/chemistry ; Wiskott-Aldrich Syndrome Protein Family/genetics ; Wiskott-Aldrich Syndrome Protein Family/metabolism
Chemical Substances	Actin-Related Protein 2-3 Complex ; Wiskott-Aldrich Syndrome Protein Family
Language	English
Publishing date	2010-06-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	207924-0
ISSN	1545-4509 ; 0066-4154
ISSN (online)	1545-4509
ISSN	0066-4154
DOI	10.1146/annurev.biochem.77.060407.135452
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Article ; Online: Purification of native Arp2/3 complex from bovine thymus.

Doolittle, Lynda K / Rosen, Michael K / Padrick, Shae B

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

2013 Volume 1046, Page(s) 231–250

Abstract: The Arp2/3 complex is an actin filament nucleator involved in cell motility and vesicle trafficking. Owing to the role the complex plays in important and fundamental cell biological processes, the purified complex is used in biochemical assays, ... ...

Abstract	The Arp2/3 complex is an actin filament nucleator involved in cell motility and vesicle trafficking. Owing to the role the complex plays in important and fundamental cell biological processes, the purified complex is used in biochemical assays, reconstituted motility assays, and structural biology. As this is a eukaryotic complex assembled from seven polypeptides, the complex is purified from eukaryotic sources. Described here is a detailed method for purification of the complex from a mammalian tissue, bovine thymus.
MeSH term(s)	Actin Cytoskeleton/chemistry ; Actin Cytoskeleton/metabolism ; Actin-Related Protein 2-3 Complex/chemistry ; Actin-Related Protein 2-3 Complex/isolation & purification ; Animals ; Cattle ; Cell Migration Assays ; Molecular Biology/methods ; Peptides/isolation & purification
Chemical Substances	Actin-Related Protein 2-3 Complex ; Peptides
Language	English
Publishing date	2013-07-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-62703-538-5_14
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