FRMPD2

Last update 08 May 2025

Basic Info

Synonyms

FERM and PDZ domain containing 2, FERM and PDZ domain-containing protein 2, FRMPD2

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Introduction

Functions as a scaffold protein and likely plays a role in N-methyl-D-aspartic acid receptor (NMDAR)-mediated synaptic excitatory transmission (By similarity). May be involved in synapse formation in cone photoreceptor cells (By similarity). May play a role in the regulation of tight junction formation (PubMed:19706687). Binds phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) (PubMed:19706687). May play a role in the regulation of NOD2-mediated NF-kappa-B activation in immune response (PubMed:23213202).

100 Clinical Results associated with FRMPD2

100 Translational Medicine associated with FRMPD2

0 Patents (Medical) associated with FRMPD2

Literatures (Medical) associated with FRMPD2

01 Aug 2019·Biochemical and Biophysical Research Communications

The second PDZ domain of scaffold protein Frmpd2 binds to GluN2A of NMDA receptors

Article

Author: Wang, Tao ; Zhang, Qijun ; Lu, Xi

The scaffold proteins Frmpd2 is localized at the basolateral membranes of polarized epithelial cells and associated with tight junction formation. In this report, we found that the Frmpd2 is specifically expressed at postsynaptic membrane. By using of co-immunoprecipitation and GST pull-down, Frmpd2 was reported to interact with postsynaptic excitatory N-methyl-d-aspartic acid (NMDA) receptors in vivo and in vitro. In addition, we demonstrated that the second PDZ (PDZ2) domain but not the first or third PDZ domain of Frmpd2 binds to the C-terminus of GluN2A and GluN2B, two subunits of NMDA receptors. By surface plasmon resonance, the affinity of Frmpd2-isolated PDZ2 to GluN2A and GluN2B was identified, which indicates that the interaction of Frmpd2 to GluN2A subunit is more strongly than that to GluN2B subunit. The crystal structure of the PDZ2 domain of the mouse homologue of Frmpd2 was further solved. Some amino acid residues of the PDZ2 structure are supposed to associate with the GluN2A binding. Our study suggests that the scaffold protein Frmpd2 is probably involved in synaptic NMDA receptors-mediated neural excitatory and neurotoxicity in a PDZ2 domain-dependent manner.

01 Mar 2018·Cell ReportsQ1 · BIOLOGY

Lrit1, a Retinal Transmembrane Protein, Regulates Selective Synapse Formation in Cone Photoreceptor Cells and Visual Acuity

Q1 · BIOLOGY

ArticleOA

Author: Kozuka, Takashi ; Matsushita, Kenji ; Omori, Yoshihiro ; Chaya, Taro ; Ueno, Akiko ; Watanabe, Satoshi ; Kajimura, Naoko ; Okada, Yasushi ; Sugita, Yuko ; Kon, Tetsuo ; Kuwahara, Ryusuke ; Yoshida, Satoyo ; Furukawa, Takahisa

In the vertebrate retina, cone photoreceptors play crucial roles in photopic vision by transmitting light-evoked signals to ON- and/or OFF-bipolar cells. However, the mechanisms underlying selective synapse formation in the cone photoreceptor pathway remain poorly understood. Here, we found that Lrit1, a leucine-rich transmembrane protein, localizes to the photoreceptor synaptic terminal and regulates the synaptic connection between cone photoreceptors and cone ON-bipolar cells. Lrit1-deficient retinas exhibit an aberrant morphology of cone photoreceptor pedicles, as well as an impairment of signal transmission from cone photoreceptors to cone ON-bipolar cells. Furthermore, we demonstrated that Lrit1 interacts with Frmpd2, a photoreceptor scaffold protein, and with mGluR6, an ON-bipolar cell-specific glutamate receptor. Additionally, Lrit1-null mice showed visual acuity impairments in their optokinetic responses. These results suggest that the Frmpd2-Lrit1-mGluR6 axis regulates selective synapse formation in cone photoreceptors and is essential for normal visual function.

26 Dec 2012·Proceedings of the National Academy of SciencesQ1 · CROSS-FIELD

RNAi screening identifies mediators of NOD2 signaling: Implications for spatial specificity of MDP recognition

Q1 · CROSS-FIELD

Article

Author: Schreiber, Stefan ; Häsler, Robert ; Lipinski, Simone ; Till, Andreas ; Erdmann, Kai Sven ; Aden, Konrad ; Rosenstiel, Philip ; Arlt, Alexander ; Hagemann, Nina ; Grabe, Nils ; Paulsen, Maren ; Billmann-Born, Susanne ; Jacobs, Gunnar ; Kraemer, Lars

The intracellular nucleotide-binding oligomerization domain-2 (NOD2) receptor detects bacteria-derived muramyl dipeptide (MDP) and activates the transcription factor NF-κB. Here we describe the regulatome of NOD2 signaling using a systematic RNAi screen. Using three consecutive screens, we identified a set of 20 positive NF-κB regulators including the known pathway members RIPK2, RELA, and BIRC4 (XIAP) as well as FRMPD2 (FERM and PDZ domain-containing 2). FRMPD2 interacts with NOD2 via leucine-rich repeats and forms a complex with the membrane-associated protein ERBB2IP. We demonstrate that FRMPD2 spatially assembles the NOD2-signaling complex, hereby restricting NOD2-mediated immune responses to the basolateral compartment of polarized intestinal epithelial cells. We show that genetic truncation of the NOD2 leucine-rich repeat domain, which is associated with Crohn disease, impairs the interaction with FRMPD2, and that intestinal inflammation leads to down-regulation of FRMPD2 . These results suggest a structural mechanism for how polarity of epithelial cells acts on intestinal NOD-like receptor signaling to mediate spatial specificity of bacterial recognition and control of immune responses.

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FRMPD2

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