GATD1

Last update 08 May 2025

Basic Info

Synonyms

FLJ34283, GATD1, glutamine amidotransferase class 1 domain containing 1

+ [3]

Introduction

Component of the FERRY complex (Five-subunit Endosomal Rab5 and RNA/ribosome intermediary) (PubMed:37267905, PubMed:37267906). The FERRY complex directly interacts with mRNAs and RAB5A, and functions as a RAB5A effector involved in the localization and the distribution of specific mRNAs most likely by mediating their endosomal transport. The complex recruits mRNAs and ribosomes to early endosomes through direct mRNA-interaction (PubMed:37267905).

100 Clinical Results associated with GATD1

100 Translational Medicine associated with GATD1

0 Patents (Medical) associated with GATD1

Literatures (Medical) associated with GATD1

15 Mar 2025·Biology Open

Neurogenetic disorders associated with mutations in the FERRY complex: a novel disease class?

Review

Author: Riffe, R. Madison ; Downes, Gerald B.

ABSTRACTThe five-subunit endosomal Rab5 and RNA/ribose intermediary (FERRY) complex is a newly described protein complex consisting of TBCK, PPP1R21, FERRY3 (previously C12orf4), CRYZL1, and GATD1. The FERRY complex is proposed to function as a Rab5 effector to shuttle mRNA to the cell periphery for local translation, a process especially important in cells with far reaching processes. Interestingly, three members of the FERRY complex are associated with ultra-rare neurogenetic disorders. Mutation of TBCK causes TBCK syndrome, mutation of PPP1R21 is associated with PPP1R21-related intellectual disability, and mutation of FERRY3 results in an autosomal recessive intellectual disability. Neurologic disorders have yet to be associated with mutation of GATD1 or CRYZL1. Here, we provide a review of each FERRY complex-related neurologic disorder and draw clinical comparisons between the disease states. We also discuss data from the current cellular and animal models available to study these disorders, which is notably disparate and scattered across different cell types and systems. Taken together, we explore the possibility that these three diseases may represent one shared disease class, which could be further understood by combining and comparing known information about each individual disease. If true, this could have substantial implications on our understanding of the cellular role of the FERRY complex and on treatment strategies for affected individuals, allowing researchers, clinicians, and patient organizations to maximize the utility of research efforts and resources to support patients with these disorders.

01 Feb 2024·Modern Pathology

Sarcomas With RAD51B Fusions Are Associated With a Heterogeneous Phenotype

Article

Author: Stenzinger, Albrecht ; Nucci, Marisa ; Dermawan, Josephine ; Torrence, Dianne ; Sharma, Aarti ; Chiang, Sarah ; Oliva, Esther ; Chang, Hsin-Yi ; Antonescu, Cristina ; Dickson, Brendan ; Mechtersheimer, Gunhild ; Turashvili, Gulisa ; Kirchner, Martina

RAD51B-rearranged sarcomas are rare neoplasms that exhibit a heterogeneous morphology. To date, 6 cases have been reported, all involving the uterus, including 4 perivascular epithelioid cell tumors (PEComas) and 2 leiomyosarcomas (LMS). In this study, we describe the morphologic, immunohistochemical, and molecular features of 8 additional sarcomas with RAD51B rearrangement, including the first extrauterine example. All patients were women with a median age of 57 years at presentation. Seven tumors originated in the uterus, and one in the lower extremity soft tissue, with a median tumor size of 12 cm. Histologically, 4 tumors showed predominantly spindle cell morphology with eosinophilic fibrillary cytoplasm, with or without nuclear pleomorphism, whereas 2 tumors exhibited pleomorphic epithelioid cells, featuring clear to eosinophilic, granular cytoplasm. Two neoplasms exhibited undifferentiated cytomorphology, including one with uniform small blue round cells. All tumors showed high-grade cytologic atypia and high mitotic activity (median: 30/10 high-power fields), whereas coagulative necrosis was noted in 6 cases and lymphovascular invasion in 2. By immunohistochemistry, 2 showed myoid and melanocytic markers in keeping with PEComa, whereas 4 cases were only positive for smooth muscle markers consistent with LMS (including 3 myxoid). The remaining 2 cases had a nonspecific immunoprofile. Five cases tested by targeted RNA sequencing (Archer FusionPlex, Illumina TruSight) showed different fusion partners (HMGA2, PDDC1, and CEP170). RAD51B rearrangements were identified by FISH in the remaining 3 cases. Targeted DNA sequencing in 2 cases was negative for TSC gene alterations. Clinical outcome, available in 5 patients (median follow-up, 19 months), revealed 3 local recurrences, 2 lung metastases, and 4 deaths due to disease. Our results expand the spectrum of sarcomas with RAD51B fusions, demonstrating variable clinical presentations, morphologic spectrum, and fusion partners. These tumors have a predilection for a uterine location, with either LMS, PEComa, or undifferentiated phenotypes, and are associated with an aggressive clinical course.

15 Jul 2023·International journal of biological macromolecules

Optimizing glycation control in diabetes: An integrated approach for inhibiting nonenzymatic glycation reactions of biological macromolecules.

Review

Author: Sun, Xiaodong ; Hou, Ningning ; Kan, Chengxia ; Liu, Yongping ; Qiu, Hongyan ; Shi, Junfeng ; Song, Hongwei ; Han, Jing ; Ma, Hongyan

Diabetes is a multifactorial disorder that increases mortality and disability due to its complications. A key driver of these complications is nonenzymatic glycation, which generates advanced glycation end-products (AGEs) that impair tissue function. Therefore, effective nonenzymatic glycation prevention and control strategies are urgently needed. This review comprehensively describes the molecular mechanisms and pathological consequences of nonenzymatic glycation in diabetes and outlines various anti-glycation strategies, such as lowering plasma glucose, interfering with the glycation reaction, and degrading early and late glycation products. Diet, exercise, and hypoglycemic medications can reduce the onset of high glucose at the source. Glucose or amino acid analogs such as flavonoids, lysine and aminoguanidine competitively bind to proteins or glucose to block the initial nonenzymatic glycation reaction. In addition, deglycation enzymes such as amadoriase, fructosamine-3-kinase, parkinson's disease protein, glutamine amidotransferase-like class 1 domain-containing 3A and terminal FraB deglycase can eliminate existing nonenzymatic glycation products. These strategies involve nutritional, pharmacological, and enzymatic interventions that target different stages of nonenzymatic glycation. This review also emphasizes the therapeutic potential of anti-glycation drugs for preventing and treating diabetes complications.

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GATD1

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