Structure of an L27 Domain Heterotrimer from Cell Polarity Complex Patj/Pals1/Mals2 Reveals Mutually Independent L27 Domain Assembly Mode

Zhang, Jinxiu; Yang, Xue; Wang, Zheng; Zhou, Hao; Xie, Xiao‐Bi; Shen, Yuequan; Long, Jiafu

doi:10.1074/jbc.m111.321216

Cited by 16 publications

(8 citation statements)

References 35 publications

(38 reference statements)

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“…Similarly, we found that CDK4 binds to the N-terminal lobe of Cyclin D1 and to the first 4 Ankyrin repeats of p19Ink4d, that Cyclin D3 binds to the CDI domain of p27Kip1, and that the human Pals1 homologue MPP5 binds to the L27 domain of LIN7. In all cases, this is in accordance with the published interaction sites. − …”

Section: Resultssupporting

confidence: 90%

Identification of Human Protein Interaction Domains using an ORFeome-based Yeast Two-hybrid Fragment Library

et al. 2013

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Physical interactions between proteins are essential for biological processes. Hence, there have been major efforts to elucidate the complete networks of protein-protein interactions, or "interactomes", of various organisms. Detailed descriptions of protein interaction networks should include information on the discrete domains that mediate these interactions, yet most large-scale efforts model interactions between whole proteins only. We previously developed a yeast two-hybrid-based strategy to systematically map interaction domains and generated a domain-based interactome network for 750 proteins involved in C. elegans early embryonic development. Here, we expand the concept of Y2H-based interaction domain mapping to the genome-wide level. We generated a human fragment library by randomly fragmenting the full-length open reading frames (ORFs) present in the human ORFeome collection. Screens using several proteins required for cell division or polarity establishment as baits demonstrate the ability to accurately identify interaction domains for human proteins using this approach, while the experimental quality of the Y2H data was independently verified in coaffinity purification assays. The library generation strategy can easily be adapted to generate libraries from full-length ORF collections of other organisms.

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Section: Resultssupporting

confidence: 90%

Identification of Human Protein Interaction Domains using an ORFeome-based Yeast Two-hybrid Fragment Library

et al. 2013

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“…A crystal structure of a heterotrimeric complex formed by the N-terminal L27 domain of PATJ, the N-terminal tandem L27 domains of PALS1, and the N-terminal L27 domain of MALS2 (mammalian homolog-2 of Lin-7) revealed an assembly of two cognate pairs of heterodimeric L27 domains. This structure is thought to reveal a novel mechanism for tandem L27 domain-mediated supramolecular complex assembly [116].…”

Section: Structural Insight Into Tight-junction Proteins Their Domentioning

confidence: 99%

Structural Features of Tight-Junction Proteins

Heinemann

Schuetz

2019

IJMS

124

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Tight junctions are complex supramolecular entities composed of integral membrane proteins, membrane-associated and soluble cytoplasmic proteins engaging in an intricate and dynamic system of protein–protein interactions. Three-dimensional structures of several tight-junction proteins or their isolated domains have been determined by X-ray crystallography, nuclear magnetic resonance spectroscopy, and cryo-electron microscopy. These structures provide direct insight into molecular interactions that contribute to the formation, integrity, or function of tight junctions. In addition, the known experimental structures have allowed the modeling of ligand-binding events involving tight-junction proteins. Here, we review the published structures of tight-junction proteins. We show that these proteins are composed of a limited set of structural motifs and highlight common types of interactions between tight-junction proteins and their ligands involving these motifs.

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“…Previous studies have shown that PATJ is multi-domain scaffold protein that binds to the apical polarity crumbs-complex via its N-terminal L27 37 . PATJ depletion via RNAi has been shown to cause a delay in tight junction formation 25,38 .…”

Section: Introductionmentioning

confidence: 99%

Wetting of junctional condensates along the apical interface promotes tight junction belt formation

Pombo‐García

Martin-Lemaitre

Honigmann

2022

Preprint

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Biomolecular condensates enable cell compartmentalization by acting as membrane-less organelles. How cells control the interactions of condensates with other cellular structures such as membranes to drive morphological transitions remains poorly understood. Here, we studied formation of tight junctions, which initially assemble as condensates that over time elongate around the membrane cell perimeter to form a closed junctional barrier. We discovered that the elongation of junctional condensates is driven by a physical wetting process around the apical membrane interface. Using temporal proximity proteomics in combination with live and super-resolution imaging, we found that wetting is mediated by the apical protein PATJ, which promotes adhesion of condensates to the apical membrane resulting in an interface formation and linear spreading into a closed belt. Using PATJ mutations we show that apical adhesion of junctional condensates is necessary and sufficient for stable tight junction belt formation. Our results demonstrate how cells exploit the collective biophysical properties of protein condensates and membrane interfaces to shape mesoscale structures.

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Structure of an L27 Domain Heterotrimer from Cell Polarity Complex Patj/Pals1/Mals2 Reveals Mutually Independent L27 Domain Assembly Mode

Cited by 16 publications

References 35 publications

Identification of Human Protein Interaction Domains using an ORFeome-based Yeast Two-hybrid Fragment Library

Identification of Human Protein Interaction Domains using an ORFeome-based Yeast Two-hybrid Fragment Library

Structural Features of Tight-Junction Proteins

Wetting of junctional condensates along the apical interface promotes tight junction belt formation

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