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Last update 08 May 2025

STRIP1

Last update 08 May 2025

Basic Info

Synonyms

FAM40A, FAR11A, FLJ14743

+ [5]

Introduction

Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation.

Drugs associated with STRIP1

Oncolytic vaccinia virus (Hangzhou Gongchu Biotechnology)

Target

STRIP1

Mechanism

STRIP1 inhibitors

Active Org.

Hangzhou Gongchu Biotechnology Co., Ltd.

Originator Org.

Hangzhou Gongchu Biotechnology Co., Ltd.

Active Indication

High grade glioma [+10]

Inactive Indication-

Drug Highest PhasePhase 1

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with STRIP1

NCT06660056

/ RecruitingPhase 1

A Phase I Study Evaluating the Safety, Tolerability, Biodistribution and Shedding of Oncolytic Vaccinia Virus GC001, Pharmacodynamics, Immunogenicity, and Antitumor Activity of the Virus in Patient With Recurrent or Progressive Gliomas

A Phase I Study Evaluating the Safety, Tolerability, Biodistribution and Shedding of the Virus, Pharmacodynamics, Immunogenicity, and Antitumor Activity of GC001 Oncolytic Vaccinia Virus Injection in Patient With Recurrent or Progressive Gliomas .

Start Date08 Oct 2024

Sponsor / Collaborator

Hangzhou Gongchu Biotechnology Co., Ltd.

CTR20231135

/ RecruitingPhase 1

一项评估 GC001 溶瘤痘苗病毒注射液在晚期实体瘤患者中的安全性、耐受性、病毒的生物分布和脱落、药效学、免疫原性和抗肿瘤活性的 I 期临床研究

[Translation] A Phase I study evaluating the safety, tolerability, viral biodistribution and shedding, pharmacodynamics, immunogenicity, and antitumor activity of GC001 oncolytic vaccinia virus injection in patients with advanced solid tumors

评估 GC001 溶瘤痘苗病毒注射液在晚期实体瘤患者中单次给药的安全性、耐受性、病毒的生物分布和脱落、药效学、免疫原性和抗肿瘤活性

[Translation]

To evaluate the safety, tolerability, viral biodistribution and shedding, pharmacodynamics, immunogenicity, and antitumor activity of a single-dose GC001 oncolytic vaccinia virus injection in patients with advanced solid tumors

Start Date23 May 2023

Sponsor / Collaborator

Hangzhou Gongchu Biotechnology Co., Ltd.

NCT06508307

/ RecruitingPhase 1

The present trial is an open, single-arm phase I clinical study aimed at assessing the safety, tolerability, viral distribution and shedding patterns, pharmacodynamics, immunogenicity, and antitumor efficacy of GC001 oncolytic virus injection in patients with advanced solid tumors following a single administration.

Start Date26 Apr 2023

Sponsor / Collaborator

Hangzhou Gongchu Biotechnology Co., Ltd.

100 Clinical Results associated with STRIP1

100 Translational Medicine associated with STRIP1

0 Patents (Medical) associated with STRIP1

Literatures (Medical) associated with STRIP1

01 Aug 2023·Molecular biology of the cell

FARL-11 (STRIP1/2) is required for sarcomere and sarcoplasmic reticulum organization in C. elegans.

Article

Author: Qadota, Hiroshi ; Oberhauser, Andres F ; Martin, Sterling C T ; Hardin, Jeff ; Benian, Guy M

Protein phosphatase 2A (PP2A) functions in a variety of cellular contexts. PP2A can assemble into four different complexes based on the inclusion of different regulatory or targeting subunits. The B''' regulatory subunit "striatin" forms the STRIPAK complex consisting of striatin, a catalytic subunit (PP2AC), striatin-interacting protein 1 (STRIP1), and MOB family member 4 (MOB4). In yeast and Caenorhabditis elegans, STRIP1 is required for formation of the endoplasmic reticulum (ER). Because the sarcoplasmic reticulum (SR) is the highly organized muscle-specific version of ER, we sought to determine the function of the STRIPAK complex in muscle using C. elegans. CASH-1 (striatin) and FARL-11 (STRIP1/2) form a complex in vivo, and each protein is localized to SR. Missense mutations and single amino acid losses in farl-11 and cash-1 each result in similar sarcomere disorganization. A missense mutation in farl-11 shows no detectable FARL-11 protein by immunoblot, disruption of SR organization around M-lines, and altered levels of the SR Ca⁺² release channel UNC-68.

01 Mar 2021·Nature Structural & Molecular BiologyQ1 · BIOLOGY

Cryo-EM structure of the Hippo signaling integrator human STRIPAK

Q1 · BIOLOGY

Article

Author: Bai, Xiao-Chen ; Bae, Sung Jun ; Ni, Lisheng ; Jeong, Byung-Cheon ; Zhang, Xuewu ; Luo, Xuelian

The striatin-interacting phosphatase and kinase (STRIPAK) complex is a large, multisubunit protein phosphatase 2A (PP2A) assembly that integrates diverse cellular signals in the Hippo pathway to regulate cell proliferation and survival. The architecture and assembly mechanism of this critical complex are poorly understood. Using cryo-EM, we determine the structure of the human STRIPAK core comprising PP2AA, PP2AC, STRN3, STRIP1, and MOB4 at 3.2-Å resolution. Unlike the canonical trimeric PP2A holoenzyme, STRIPAK contains four copies of STRN3 and one copy of each the PP2AA-C heterodimer, STRIP1, and MOB4. The STRN3 coiled-coil domains form an elongated homotetrameric scaffold that links the complex together. An inositol hexakisphosphate (IP₆) is identified as a structural cofactor of STRIP1. Mutations of key residues at subunit interfaces disrupt the integrity of STRIPAK, causing aberrant Hippo pathway activation. Thus, STRIPAK is established as a noncanonical PP2A complex with four copies of regulatory STRN3 for enhanced signal integration.

01 Jan 2019·Archives of Medical ScienceQ4 · MEDICINE

FAM40A alters the cytoskeleton of podocytes in familial focal and segmental glomerulosclerosis by regulating F-actin and nephrin

Q4 · MEDICINE

ArticleOA

Author: Zhao, Xuezhi ; Chen, Zhou ; Zhang, Yinghui

INTRODUCTIONFamilial focal and segmental glomerulosclerosis (FFSGS) was found in a large cohort of patients in our previous study. Under the sponsorship of the National Natural Science Foundation of China, we conducted linkage analysis and full exon sequencing on the genomes of 54 patients diagnosed with FFSGS. The results revealed a FAM40A gene signature in those patients. To determine whether FAM40A was associated with podocyte lesions and whether changes in the podocyte cytoskeleton could affect podocyte function, mouse podocytes (MPs) were used in this study.MATERIAL AND METHODSFAM40A silencing, over-expression and mutant-type over-expression models of renal MPs were established, whereby roles of wild-type FAM40A and mutant FAM40A (c.1562T>C, p521M>T) in regulating the function of the MP cytoskeleton were explored by using cellular immunofluorescence, RT-qPCR and Western blot.RESULTSFAM40A was expressed and localized in MPs and significantly enriched in the nucleus and perinuclear zone. Changes of FAM40A expression altered the morphology of the MPs and their cytoskeletal organization, which was characterized by disordered distribution of F-actin, loss of the foot process architecture and the functional protein of the slit diaphragm nephrin (p < 0.05 or p < 0.01). FAM40A mutation (p521M>T) led to the formation of round and blunt morphology of the MPs and loss of the foot-process structure. In addition, expression of the cytoskeletal protein F-actin was increased and concentrated in FAM40A mutated cells, whereas the expression of nephrin decreased in those cells (p < 0.01).CONCLUSIONSFAM40A played an important role in maintaining the normal morphology and function of MPs by stabilizing the cytoskeleton of MPs. Moreover, mutant FAM40A (p521M>T) was able to alter the morphology and cytoskeleton of the MPs, and to decrease the expression of nephrin, which may be the main factor contributing to FSGS.

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