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Last update 08 May 2025

TIMMDC1

Last update 08 May 2025

Basic Info

Synonyms

C3orf1, Complex I assembly factor TIMMDC1, mitochondrial, FLJ22597

+ [5]

Introduction

Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Participates in constructing the membrane arm of complex I.

Drugs associated with TIMMDC1

WO2023010171

Patent Mining

Target

TIMMDC1

Mechanism-

Active Org.

University of Adelaide

Originator Org.

University of Adelaide

Active Indication

Nervous System Diseases

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with TIMMDC1

100 Translational Medicine associated with TIMMDC1

0 Patents (Medical) associated with TIMMDC1

Literatures (Medical) associated with TIMMDC1

02 May 2023·Brain

Neuropathological hallmarks of antenatal mitochondrial diseases with a corpus callosum defect

Article

Author: Jauny, Clémence ; Tessier, Aude ; Bole-Feysot, Christine ; Attié-Bitach, Tania ; Talhi, Naïma ; Blanchet, Patricia ; Bessières, Bettina ; Pannier, Emmanuelle ; Grotto, Sarah ; Metodiev, Metodi D ; Nitschke, Patrick ; Razavi, Ferechte ; Musizzano, Yuri ; Loeuilllet, Laurence ; Boutaud, Lucile ; Anselem, Olivia ; Rötig, Agnès ; Wells, Constance ; Amram, Daniel ; Willems, Marjolaine ; Achaiaa, Amale ; Ruzzenente, Benedetta ; Salhi, Houria

AbstractCorpus callosum defects are frequent congenital cerebral disorders caused by mutations in more than 300 genes. These include genes implicated in corpus callosum development or function, as well as genes essential for mitochondrial physiology. However, in utero corpus callosum anomalies rarely raise a suspicion of mitochondrial disease and are characterized by a very large clinical heterogeneity.Here, we report a detailed pathological and neuro-histopathological investigation of nine foetuses from four unrelated families with prenatal onset of corpus callosum anomalies, sometimes associated with other cerebral or extra-cerebral defects. Next generation sequencing allowed the identification of novel pathogenic variants in three different nuclear genes previously reported in mitochondrial diseases: TIMMDC1, encoding a Complex I assembly factor never involved before in corpus callosum defect; MRPS22, a protein of the small mitoribosomal subunit; and EARS2, the mitochondrial tRNA-glutamyl synthetase. The present report describes the antenatal histopathological findings in mitochondrial diseases and expands the genetic spectrum of antenatal corpus callosum anomalies establishing OXPHOS function as an important factor for corpus callosum biogenesis.We propose that, when observed, antenatal corpus callosum anomalies should raise suspicion of mitochondrial disease and prenatal genetic counselling should be considered.

01 Aug 2021·iScienceQ2 · CROSS-FIELD

Dissecting the concordant and disparate roles of NDUFAF3 and NDUFAF4 in mitochondrial complex I biogenesis

Q2 · CROSS-FIELD

ArticleOA

Author: Li, Hong ; Garcia, Christian ; Mishra, Bibhuti ; Liu, Tong ; Murari, Anjaneyulu ; Rhooms, Shauna-Kay ; Owusu-Ansah, Edward ; Deshong, Cassie

Distinct sub-assemblies (modules) of mitochondrial complex I (CI) are assembled with the assistance of CI Assembly Factors (CIAFs) through mechanisms that are incompletely defined. Here, using genetic analyses in Drosophila, we report that when either of the CIAFs - NDUFAF3 or NDUFAF4 - is disrupted, biogenesis of the Q-, N-, and P_P-b-modules of CI is impaired. This is due, at least in part, to the compromised integration of NDUFS3 and NDUFS5 into the Q-, and P_P-b-modules, respectively, coupled with a destabilization of another CIAF, TIMMDC1, in assembly intermediates. Notably, forced expression of NDUFAF4 rescues the biogenesis defects in the Q-module and some aspects of the defects in the P_P-b-module of CI when NDUFAF3 is disrupted. Altogether, our studies furnish new fundamental insights into the mechanism by which NDUFAF3 and NDUFAF4 regulate CI assembly and raises the possibility that certain point mutations in NDUFAF3 may be rescued by overexpression of NDUFAF4.

01 Apr 2021·Cell ReportsQ1 · BIOLOGY

A membrane arm of mitochondrial complex I sufficient to promote respirasome formation

Q1 · BIOLOGY

ArticleOA

Author: Zhu, Jingjing ; Yang, Yanling ; Lin, Zifan ; Yang, Yue ; Li, Haiyan ; Fang, Hezhi ; Xie, Jie ; Jia, Manli ; Han, Qing ; Lyu, Jianxin ; Bao, Xinzhu ; Li, Yuanyuan ; Zhao, Qiongya ; Ye, Xianglai ; Li, Xueyun

The assembly pathways of mitochondrial respirasome (supercomplex I+III₂+IV) are not fully understood. Here, we show that an early sub-complex I assembly, rather than holo-complex I, is sufficient to initiate mitochondrial respirasome assembly. We find that a distal part of the membrane arm of complex I (P_D-a module) is a scaffold for the incorporation of complexes III and IV to form a respirasome subcomplex. Depletion of P_D-a, rather than other complex I modules, decreases the steady-state levels of complexes III and IV. Both HEK293T cells lacking TIMMDC1 and patient-derived cells with disease-causing mutations in TIMMDC1 showed accumulation of this respirasome subcomplex. This suggests that TIMMDC1, previously known as a complex-I assembly factor, may function as a respirasome assembly factor. Collectively, we provide a detailed, cooperative assembly model in which most complex-I subunits are added to the respirasome subcomplex in the lateral stages of respirasome assembly.

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