The multi-PDZ domain protein-1 (MUPP-1) expression regulates cellular levels of the PALS-1/PATJ polarity complex

Assémat, Emeline; Crost, Emmanuelle H.; Ponserre, Marion; Wijnholds, Jan; Bivic, André Le; Massey-Harroche, Dominique

doi:10.1016/j.yexcr.2013.07.011

Cited by 35 publications

(41 citation statements)

References 28 publications

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“…MPDZ encodes for a protein that localizes to tight junctions [40] and may help regular planar cell polarity [41]. Previously studied in the context of addiction [42], alcohol withdrawal [43], and retinal degeneration [44], MPDZ was recently implicated as the cause of hydrocephalus in two consanguineous Saudi families [45].…”

Section: Hydrocephalus Without Major Additional Physical Features (Tamentioning

confidence: 99%

Infantile hydrocephalus: A review of epidemiology, classification and causes

Tully¹,

Dobyns²

2014

European Journal of Medical Genetics

322

246

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Hydrocephalus is a common but complex condition caused by physical or functional obstruction of CSF flow that leads to progressive ventricular dilatation. Though hydrocephalus was recently estimated to affect 1.1 in 1,000 infants, there have been few systematic assessments of the causes of hydrocephalus in this age group, which makes it a challenging condition to approach as a scientist or as a clinician. Here, we review contemporary literature on the epidemiology, classification and pathogenesis of infantile hydrocephalus. We describe the major environmental and genetic causes of hydrocephalus, with the goal of providing a framework to assess infants with hydrocephalus and guide future research.

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Section: Hydrocephalus Without Major Additional Physical Features (Tamentioning

confidence: 99%

Infantile hydrocephalus: A review of epidemiology, classification and causes

Tully¹,

Dobyns²

2014

European Journal of Medical Genetics

322

246

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“…Silencing of MPDZ expression did not alter paracellular permeability of EpH4 breast carcinoma cells (Adachi et al, 2009). However, loss of MPDZ may be compensated by increased expression of INADL (also known as InaD-like or PATJ), a structural paralogue of the MPDZ protein (Adachi et al, 2009;Assémat et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Loss of Mpdz impairs ependymal cell integrity leading to perinatal‐onset hydrocephalus in mice

et al. 2017

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Hydrocephalus is a common congenital anomaly. LCAM1 and MPDZ (MUPP1) are the only known human gene loci associated with non‐syndromic hydrocephalus. To investigate functions of the tight junction‐associated protein Mpdz, we generated mouse models. Global Mpdz gene deletion or conditional inactivation in Nestin‐positive cells led to formation of supratentorial hydrocephalus in the early postnatal period. Blood vessels, epithelial cells of the choroid plexus, and cilia on ependymal cells, which line the ventricular system, remained morphologically intact in Mpdz‐deficient brains. However, flow of cerebrospinal fluid through the cerebral aqueduct was blocked from postnatal day 3 onward. Silencing of Mpdz expression in cultured epithelial cells impaired barrier integrity, and loss of Mpdz in astrocytes increased RhoA activity. In Mpdz‐deficient mice, ependymal cells had morphologically normal tight junctions, but expression of the interacting planar cell polarity protein Pals1 was diminished and barrier integrity got progressively lost. Ependymal denudation was accompanied by reactive astrogliosis leading to aqueductal stenosis. This work provides a relevant hydrocephalus mouse model and demonstrates that Mpdz is essential to maintain integrity of the ependyma.

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“…In MCF10A cells, there are two co-existing CRB complexes, CRB3/PALS1/PATJ and CRB3/PALS1/MUPP-1. Downregulation of MUPP-1 induces an upregulation of CRB3/PALS1/PATJ complex by stabilizing PATJ, suggesting that a homeostatic balance between these two complexes are likely necessary to confer polarity [50]. MUPP-1 has been found in the heart, brain, placenta, liver, skeletal muscle, kidney, pancreas and testis [22].…”

Section: Crb Complexmentioning

confidence: 99%

Cell polarity proteins and spermatogenesis

Gao

Xiao²,

Lui

et al. 2016

Seminars in Cell & Developmental Biology

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When the cross-section of a seminiferous tubule from adult rat testes is examined microscopically, Sertoli cells and germ cells in the seminiferous epithelium are notably polarized. For instance, Sertoli cell nuclei are found near the basement membrane; tight junction (TJ), basal ectoplasmic specialization (basal ES, a testis-specific actin-rich anchoring junction), gap junction (GJ) and desmosome that constitute the blood-testis barrier (BTB) which divide the epithelium into the basal and adluminal (apical) compartments, are located near the tunica propria. Within the epithelium, undifferentiated spermatogonia and preleptotene spermatocytes restrictively reside in the basal compartment whereas spermatocytes and post-meiotic spermatids reside in the adluminal compartment. Furthermore, the heads of elongating/elongated spermatids point toward the basement membrane with their elongating tails toward the tubule lumen. However, the involvement of polarity proteins in this unique cellular organization, in particular the underlying molecular mechanism(s) by which polarity proteins confer cellular polarity in the seminiferous epithelium are virtually unknown until recent years. Herein, we discuss latest findings regarding the role of different polarity protein complexes or modules and how these protein complexes are working in concert to modulate Sertoli cell and spermatid polarity. These findings also illustrate polarity proteins exert their effects through the actin-based cytoskeleton mediated by actin binding and regulatory proteins, which in turn modulate adhesion protein complexes at the cell-cell interface since TJ, basal ES and GJ utilize F-actin for attachment. We also propose a hypothetical model which illustrate the antagonistic effects of these polarity proteins that provide a unique mechanism to modulate junction remodeling in the testis to support germ cell transport across the epithelium in particular the BTB during the epithelial cycle of spermatogenesis.

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The multi-PDZ domain protein-1 (MUPP-1) expression regulates cellular levels of the PALS-1/PATJ polarity complex

Cited by 35 publications

References 28 publications

Infantile hydrocephalus: A review of epidemiology, classification and causes

Infantile hydrocephalus: A review of epidemiology, classification and causes

Loss of Mpdz impairs ependymal cell integrity leading to perinatal‐onset hydrocephalus in mice

Cell polarity proteins and spermatogenesis

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