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Article ; Online: WASP family proteins: Molecular mechanisms and implications in human disease.

Kramer, Daniel A / Piper, Hannah K / Chen, Baoyu

2022 Volume 101, Issue 3, Page(s) 151244

Abstract: Proteins of the Wiskott-Aldrich syndrome protein (WASP) family play a central role in regulating actin cytoskeletal dynamics in a wide range of cellular processes. Genetic mutations or misregulation of these proteins are tightly associated with many ... ...

Abstract	Proteins of the Wiskott-Aldrich syndrome protein (WASP) family play a central role in regulating actin cytoskeletal dynamics in a wide range of cellular processes. Genetic mutations or misregulation of these proteins are tightly associated with many diseases. The WASP-family proteins act by transmitting various upstream signals to their conserved WH2-Central-Acidic (WCA) peptide sequence at the C-terminus, which in turn binds to the Arp2/3 complex to stimulate the formation of branched actin networks at membranes. Despite this common feature, the regulatory mechanisms and cellular functions of distinct WASP-family proteins are very different. Here, we summarize and clarify our current understanding of WASP-family proteins and how disruption of their functions is related to human disease.
MeSH term(s)	Actin-Related Protein 2-3 Complex/genetics ; Actin-Related Protein 2-3 Complex/metabolism ; Actins/metabolism ; Cytoskeleton/metabolism ; Humans ; Wiskott-Aldrich Syndrome Protein Family/genetics ; Wiskott-Aldrich Syndrome Protein Family/metabolism
Chemical Substances	Actin-Related Protein 2-3 Complex ; Actins ; Wiskott-Aldrich Syndrome Protein Family
Language	English
Publishing date	2022-06-01
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.2022.151244
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Article ; Online: A two-step actin polymerization mechanism drives dendrite branching.

Shi, Rebecca / Kramer, Daniel A / Chen, Baoyu / Shen, Kang

Neural development

2021 Volume 16, Issue 1, Page(s) 3

Abstract: Background: Dendrite morphogenesis plays an essential role in establishing the connectivity and receptive fields of neurons during the development of the nervous system. To generate the diverse morphologies of branched dendrites, neurons use external ... ...

Abstract	Background: Dendrite morphogenesis plays an essential role in establishing the connectivity and receptive fields of neurons during the development of the nervous system. To generate the diverse morphologies of branched dendrites, neurons use external cues and cell surface receptors to coordinate intracellular cytoskeletal organization; however, the molecular mechanisms of how this signaling forms branched dendrites are not fully understood. Methods: We performed in vivo time-lapse imaging of the PVD neuron in C. elegans in several mutants of actin regulatory proteins, such as the WAVE Regulatory Complex (WRC) and UNC-34 (homolog of Enabled/Vasodilator-stimulated phosphoprotein (Ena/VASP)). We examined the direct interaction between the WRC and UNC-34 and analyzed the localization of UNC-34 in vivo using transgenic worms expressing UNC-34 fused to GFP. Results: We identify a stereotyped sequence of morphological events during dendrite outgrowth in the PVD neuron in C. elegans. Specifically, local increases in width ("swellings") give rise to filopodia to facilitate a "rapid growth and pause" mode of growth. In unc-34 mutants, filopodia fail to form but swellings are intact. In WRC mutants, dendrite growth is largely absent, resulting from a lack of both swelling and filopodia formation. We also found that UNC-34 can directly bind to the WRC. Disrupting this binding by deleting the UNC-34 EVH1 domain prevented UNC-34 from localizing to swellings and dendrite tips, resulting in a stunted dendritic arbor and reduced filopodia outgrowth. Conclusions: We propose that regulators of branched and linear F-actin cooperate to establish dendritic branches. By combining our work with existing literature, we propose that the dendrite guidance receptor DMA-1 recruits the WRC, which polymerizes branched F-actin to generate "swellings" on a mother dendrite. Then, WRC recruits the actin elongation factor UNC-34/Ena/VASP to initiate growth of a new dendritic branch from the swelling, with the help of the actin-binding protein UNC-115/abLIM. Extension of existing dendrites also proceeds via swelling formation at the dendrite tip followed by UNC-34-mediated outgrowth. Following dendrite initiation and extension, the stabilization of branches by guidance receptors further recruits WRC, resulting in an iterative process to build a complex dendritic arbor.
MeSH term(s)	Actins ; Animals ; Caenorhabditis elegans ; Caenorhabditis elegans Proteins/genetics ; Dendrites ; Membrane Proteins ; Nerve Tissue Proteins ; Polymerization
Chemical Substances	Actins ; Caenorhabditis elegans Proteins ; DMA-1 protein, C elegans ; Membrane Proteins ; Nerve Tissue Proteins ; unc-34 protein, C elegans
Language	English
Publishing date	2021-07-19
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2254847-6
ISSN	1749-8104 ; 1749-8104
ISSN (online)	1749-8104
ISSN	1749-8104
DOI	10.1186/s13064-021-00154-0
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Article ; Online: The intrinsically disordered cytoplasmic tail of a dendrite branching receptor uses two distinct mechanisms to regulate the actin cytoskeleton.

Kramer, Daniel A / Narvaez-Ortiz, Heidy Y / Patel, Urval / Shi, Rebecca / Shen, Kang / Nolen, Brad J / Roche, Julien / Chen, Baoyu

eLife

2023 Volume 12

Abstract: Dendrite morphogenesis is essential for neural circuit formation, yet the molecular mechanisms underlying complex dendrite branching remain elusive. Previous studies on the highly ... ...

Abstract	Dendrite morphogenesis is essential for neural circuit formation, yet the molecular mechanisms underlying complex dendrite branching remain elusive. Previous studies on the highly branched
MeSH term(s)	Animals ; Actins/metabolism ; Actin Cytoskeleton/metabolism ; Carrier Proteins/metabolism ; Actin-Related Protein 2-3 Complex/metabolism ; Membrane Proteins/metabolism ; Caenorhabditis elegans/metabolism ; Dendrites/metabolism
Chemical Substances	Actins ; Carrier Proteins ; Actin-Related Protein 2-3 Complex ; Membrane Proteins
Language	English
Publishing date	2023-08-09
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.88492
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Article: Structural basis for Retriever-SNX17 assembly and endosomal sorting.

Singla, Amika / Boesch, Daniel J / Joyce Fung, Ho Yee / Ngoka, Chigozie / Enriquez, Avery S / Song, Ran / Kramer, Daniel A / Han, Yan / Juneja, Puneet / Billadeau, Daniel D / Bai, Xiaochen / Chen, Zhe / Turer, Emre E / Burstein, Ezra / Chen, Baoyu

bioRxiv : the preprint server for biology

2024

Abstract: During endosomal recycling, Sorting Nexin 17 (SNX17) facilitates the transport of numerous membrane cargo proteins by tethering them to the Retriever complex. Despite its importance, the mechanisms underlying this interaction have remained elusive. Here, ...

Abstract	During endosomal recycling, Sorting Nexin 17 (SNX17) facilitates the transport of numerous membrane cargo proteins by tethering them to the Retriever complex. Despite its importance, the mechanisms underlying this interaction have remained elusive. Here, we report the structure of the Retriever-SNX17 complex determined using cryogenic electron microscopy (cryo-EM). Our structure reveals that the C-terminal tail of SNX17 engages with a highly conserved interface between the VPS35L and VPS26C subunits of Retriever. Through comprehensive biochemical, cellular, and proteomic analyses, we demonstrate that disrupting this interface impairs the Retriever-SNX17 interaction, subsequently affecting the recycling of SNX17-dependent cargos and altering the composition of the plasma membrane proteome. Intriguingly, we find that the SNX17-binding pocket on Retriever can be utilized by other ligands that share a consensus acidic C-terminal tail motif. By showing how SNX17 is linked to Retriever, our findings uncover a fundamental mechanism underlying endosomal trafficking of critical cargo proteins and reveal a mechanism by which Retriever can engage with other regulatory factors.
Language	English
Publishing date	2024-03-13
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.03.12.584676
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Article: Structural Organization of the Retriever-CCC Endosomal Recycling Complex.

Boesch, Daniel J / Singla, Amika / Han, Yan / Kramer, Daniel A / Liu, Qi / Suzuki, Kohei / Juneja, Puneet / Zhao, Xuefeng / Long, Xin / Medlyn, Michael J / Billadeau, Daniel D / Chen, Zhe / Chen, Baoyu / Burstein, Ezra

Research square

2023

Abstract: The recycling of membrane proteins from endosomes to the cell surface is vital for cell signaling and survival. Retriever, a trimeric complex of VPS35L, VPS26C and VPS29, together with the CCC complex comprising CCDC22, CCDC93, and COMMD proteins, plays ... ...

Abstract	The recycling of membrane proteins from endosomes to the cell surface is vital for cell signaling and survival. Retriever, a trimeric complex of VPS35L, VPS26C and VPS29, together with the CCC complex comprising CCDC22, CCDC93, and COMMD proteins, plays a crucial role in this process. The precise mechanisms underlying Retriever assembly and its interaction with CCC have remained elusive. Here, we present the first high-resolution structure of Retriever determined using cryogenic electron microscopy. The structure reveals a unique assembly mechanism, distinguishing it from its remotely related paralog, Retromer. By combining AlphaFold predictions and biochemical, cellular, and proteomic analyses, we further elucidate the structural organization of the entire Retriever-CCC complex and uncover how cancer-associated mutations disrupt complex formation and impair membrane protein homeostasis. These findings provide a fundamental framework for understanding the biological and pathological implications associated with Retriever-CCC-mediated endosomal recycling.
Language	English
Publishing date	2023-06-16
Publishing country	United States
Document type	Preprint
DOI	10.21203/rs.3.rs-3026818/v1
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Article: Structural Organization of the Retriever-CCC Endosomal Recycling Complex.

bioRxiv : the preprint server for biology

2023

Abstract	The recycling of membrane proteins from endosomes to the cell surface is vital for cell signaling and survival. Retriever, a trimeric complex of VPS35L, VPS26C and VPS29, together with the CCC complex comprising CCDC22, CCDC93, and COMMD proteins, plays a crucial role in this process. The precise mechanisms underlying Retriever assembly and its interaction with CCC have remained elusive. Here, we present the first high-resolution structure of Retriever determined using cryogenic electron microscopy. The structure reveals a unique assembly mechanism, distinguishing it from its remotely related paralog, Retromer. By combining AlphaFold predictions and biochemical, cellular, and proteomic analyses, we further elucidate the structural organization of the entire Retriever-CCC complex and uncover how cancer-associated mutations disrupt complex formation and impair membrane protein homeostasis. These findings provide a fundamental framework for understanding the biological and pathological implications associated with Retriever-CCC-mediated endosomal recycling.
Language	English
Publishing date	2023-06-07
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.06.06.543888
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Article ; Online: Structural organization of the retriever-CCC endosomal recycling complex.

Nature structural & molecular biology

2023

Abstract: The recycling of membrane proteins from endosomes to the cell surface is vital for cell signaling and survival. Retriever, a trimeric complex of vacuolar protein-sorting-associated protein (VPS)35L, VPS26C and VPS29, together with the CCC complex ... ...

Abstract	The recycling of membrane proteins from endosomes to the cell surface is vital for cell signaling and survival. Retriever, a trimeric complex of vacuolar protein-sorting-associated protein (VPS)35L, VPS26C and VPS29, together with the CCC complex comprising coiled-coil domain-containing (CCDC)22, CCDC93 and copper metabolism domain-containing (COMMD) proteins, plays a crucial role in this process. The precise mechanisms underlying retriever assembly and its interaction with CCC have remained elusive. Here, we present a high-resolution structure of retriever in humans determined using cryogenic electron microscopy. The structure reveals a unique assembly mechanism, distinguishing it from its remotely related paralog retromer. By combining AlphaFold predictions and biochemical, cellular and proteomic analyses, we further elucidate the structural organization of the entire retriever-CCC complex across evolution and uncover how cancer-associated mutations in humans disrupt complex formation and impair membrane protein homeostasis. These findings provide a fundamental framework for understanding the biological and pathological implications associated with retriever-CCC-mediated endosomal recycling.
Language	English
Publishing date	2023-12-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	2126708-X
ISSN	1545-9985 ; 1545-9993
ISSN (online)	1545-9985
ISSN	1545-9993
DOI	10.1038/s41594-023-01184-4
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Article ; Online: Arf GTPase activates the WAVE regulatory complex through a distinct binding site.

Yang, Sheng / Tang, Yubo / Liu, Yijun / Brown, Abbigale J / Schaks, Matthias / Ding, Bojian / Kramer, Daniel A / Mietkowska, Magdalena / Ding, Li / Alekhina, Olga / Billadeau, Daniel D / Chowdhury, Saikat / Wang, Junmei / Rottner, Klemens / Chen, Baoyu

Science advances

2022 Volume 8, Issue 50, Page(s) eadd1412

Abstract: Cross-talk between Rho- and Arf-family guanosine triphosphatases (GTPases) plays an important role in linking the actin cytoskeleton to membrane protrusions, organelle morphology, and vesicle trafficking. The central actin regulator, WAVE regulatory ... ...

Abstract	Cross-talk between Rho- and Arf-family guanosine triphosphatases (GTPases) plays an important role in linking the actin cytoskeleton to membrane protrusions, organelle morphology, and vesicle trafficking. The central actin regulator, WAVE regulatory complex (WRC), integrates Rac1 (a Rho-family GTPase) and Arf signaling to promote Arp2/3-mediated actin polymerization in many processes, but how WRC senses Arf signaling is unknown. Here, we have reconstituted a direct interaction between Arf and WRC. This interaction is greatly enhanced by Rac1 binding to the D site of WRC. Arf1 binds to a previously unidentified, conserved surface on the Sra1 subunit of WRC, which, in turn, drives WRC activation using a mechanism distinct from that of Rac1. Mutating the Arf binding site abolishes Arf1-WRC interaction, disrupts Arf1-mediated WRC activation, and impairs lamellipodia formation and cell migration. This work uncovers a new mechanism underlying WRC activation and provides a mechanistic foundation for studying how WRC-mediated actin polymerization links Arf and Rac signaling in cells.
Language	English
Publishing date	2022-12-14
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.add1412
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Article ; Online: A Dendritic Guidance Receptor Complex Brings Together Distinct Actin Regulators to Drive Efficient F-Actin Assembly and Branching.

Zou, Wei / Dong, Xintong / Broederdorf, Timothy R / Shen, Ao / Kramer, Daniel A / Shi, Rebecca / Liang, Xing / Miller, David M / Xiang, Yang K / Yasuda, Ryohei / Chen, Baoyu / Shen, Kang

Developmental cell

2018 Volume 45, Issue 3, Page(s) 362–375.e3

Abstract: Proper morphogenesis of dendrites plays a fundamental role in the establishment of neural circuits. The molecular mechanism by which dendrites grow highly complex branches is not well understood. Here, using the Caenorhabditis elegans PVD neuron, we ... ...

Abstract	Proper morphogenesis of dendrites plays a fundamental role in the establishment of neural circuits. The molecular mechanism by which dendrites grow highly complex branches is not well understood. Here, using the Caenorhabditis elegans PVD neuron, we demonstrate that high-order dendritic branching requires actin polymerization driven by coordinated interactions between two membrane proteins, DMA-1 and HPO-30, with their cytoplasmic interactors, the RacGEF TIAM-1 and the actin nucleation promotion factor WAVE regulatory complex (WRC). The dendrite branching receptor DMA-1 directly binds to the PDZ domain of TIAM-1, while the claudin-like protein HPO-30 directly interacts with the WRC. On dendrites, DMA-1 and HPO-30 form a receptor-associated signaling complex to bring TIAM-1 and the WRC to close proximity, leading to elevated assembly of F-actin needed to drive high-order dendrite branching. The synergistic activation of F-actin assembly by scaffolding distinct actin regulators might represent a general mechanism in promoting complex dendrite arborization.
MeSH term(s)	Actin Cytoskeleton/genetics ; Actin Cytoskeleton/metabolism ; Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/growth & development ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Membrane/metabolism ; Dendrites/genetics ; Dendrites/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Morphogenesis/physiology ; Neurogenesis/physiology ; Sensory Receptor Cells/metabolism ; Signal Transduction
Chemical Substances	Caenorhabditis elegans Proteins ; DMA-1 protein, C elegans ; Membrane Proteins ; wve-1 protein, C elegans
Language	English
Publishing date	2018-05-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2018.04.008
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Zs.MG 76: Show issues

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