| PALS1 is a key regulator of the lateral distribution of tight junction proteins in renal epithelial cells. | PALS1 is a key regulator of the lateral distribution of tight junction proteins in renal epithelial cells.
Groh AC, Möller-Kerutt A, Gilhaus K, Höffken V, Nedvetsky P, Kleimann S, Behrens M, Ghosh S, Hansen U, Krahn MP, Ebnet K, Pavenstädt H, Ludwig A, Weide T. | 02/29/2024 |
| De novo variants in MPP5 cause global developmental delay and behavioral changes. | De novo variants in MPP5 cause global developmental delay and behavioral changes.
Sterling N, Duncan AR, Park R, Koolen DA, Shi J, Cho SH, Benke PJ, Grant PE, Genetti CA, VanNoy GE, Juusola J, McWalter K, Parboosingh JS, Lamont RE, Bernier FP, Smith C, Harris DJ, Stegmann APA, Innes AM, Kim S, Agrawal PB., Free PMC Article | 09/4/2021 |
| Pals1 haploinsufficiency in mouse kidneys associated with the upregulation of Hippo pathway target genes and marker genes of TGF-beta signaling, including biomarkers of renal diseases. These findings support a link between apical polarity proteins and renal diseases, especially renal cyst diseases | Pals1 Haploinsufficiency Results in Proteinuria and Cyst Formation.
Weide T, Vollenbröker B, Schulze U, Djuric I, Edeling M, Bonse J, Hochapfel F, Panichkina O, Wennmann DO, George B, Kim S, Daniel C, Seggewiß J, Amann K, Kriz W, Krahn MP, Pavenstädt H., Free PMC Article | 09/2/2017 |
| This study identifies Pals1 as a novel intrinsic factor that regulates the generation of cerebellar cells and Pals1 deficiency as a potential inhibitor of overactive mitogenic signaling. | The apical complex protein Pals1 is required to maintain cerebellar progenitor cells in a proliferative state.
Park JY, Hughes LJ, Moon UY, Park R, Kim SB, Tran K, Lee JS, Cho SH, Kim S., Free PMC Article | 07/30/2016 |
| This paper reveals the role of the canonical polarity protein Pals1 in radial sorting of axons by Schwann cells. | The Polarity Protein Pals1 Regulates Radial Sorting of Axons.
Zollinger DR, Chang KJ, Baalman K, Kim S, Rasband MN., Free PMC Article | 10/10/2015 |
| Data show the deletion of Pals1 leads to the disruption of the apical localization of Crb polarity complex proteins Crb1, Crb2 and Crb3 in retinal progenitors and the adult retina. | Genetic ablation of Pals1 in retinal progenitor cells models the retinal pathology of Leber congenital amaurosis.
Cho SH, Kim JY, Simons DL, Song JY, Le JH, Swindell EC, Jamrich M, Wu SM, Kim S., Free PMC Article | 10/13/2012 |
| Genetic study demonstrates a near-complete abrogation of cortical development in the absence of the apical complex protein Pals1. Despite the absence of most cortical structures, Pals1 CKO mice survive and display relatively normal health. | The apical complex couples cell fate and cell survival to cerebral cortical development.
Kim S, Lehtinen MK, Sessa A, Zappaterra MW, Cho SH, Gonzalez D, Boggan B, Austin CA, Wijnholds J, Gambello MJ, Malicki J, LaMantia AS, Broccoli V, Walsh CA., Free PMC Article | 05/10/2010 |
| the importance of a conserved Crumbs-MPP5-EPB41L5 polarity complex in mammals for separation of the apical and basolateral domains through specialized cell-cell junctions | FERM protein EPB41L5 is a novel member of the mammalian CRB-MPP5 polarity complex.
Gosens I, Sessa A, den Hollander AI, Letteboer SJ, Belloni V, Arends ML, Le Bivic A, Cremers FP, Broccoli V, Roepman R. | 01/21/2010 |
| analysis of structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins | A unified assembly mode revealed by the structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins.
Feng W, Long JF, Zhang M., Free PMC Article | 01/21/2010 |
| RNA interference-induced silencing of the Crb1-interacting-protein Pals1 (protein associated with Lin7; Mpp5) in Muller glial cells resulted in loss of Crb1, Crb2, Mupp1 and Veli3 protein localization and partial loss of Crb3. | Pals1/Mpp5 is required for correct localization of Crb1 at the subapical region in polarized Muller glia cells.
van Rossum AG, Aartsen WM, Meuleman J, Klooster J, Malysheva A, Versteeg I, Arsanto JP, Le Bivic A, Wijnholds J. | 01/21/2010 |
| association of Veli3 with MPP5 suggests that the MAGUKs recruit Veli3 and its binding partners to different cellular regions of the retina where they may participate in the organization of specialized intercellular junctions. | Membrane-associated guanylate kinase proteins MPP4 and MPP5 associate with Veli3 at distinct intercellular junctions of the neurosensory retina.
Stöhr H, Molday LL, Molday RS, Weber BH, Biedermann B, Reichenbach A, Krämer F. | 01/21/2010 |