OCIAD1

Last update 08 May 2025

Basic Info

Synonyms

Asrij, FLJ20455, OCIA

+ [6]

Introduction

Maintains stem cell potency (By similarity). Increases STAT3 phosphorylation and controls ERK phosphorylation (By similarity). May act as a scaffold, increasing STAT3 recruitment onto endosomes (By similarity). Involved in integrin-mediated cancer cell adhesion and colony formation in ovarian cancer (PubMed:20515946).

100 Clinical Results associated with OCIAD1

100 Translational Medicine associated with OCIAD1

0 Patents (Medical) associated with OCIAD1

Literatures (Medical) associated with OCIAD1

01 Dec 2024·Cell Reports

OCIAD1 and prohibitins regulate the stability of the TIM23 protein translocase

Article

Author: Borrero-Landazabal, Mayra A ; Gosk, Aleksandra ; Serwa, Remigiusz Adam ; Jakobs, Stefan ; Maruszczak, Klaudia K ; Gulgec, Ahmet Sadik ; Wasilewski, Michal ; Chacinska, Agnieszka ; Elancheliyan, Praveenraj ; Stephan, Till ; Ngati, Sonia

Mitochondrial proteins are transported and sorted to the matrix or inner mitochondrial membrane by the presequence translocase TIM23. In yeast, this essential and highly conserved machinery is composed of the core subunits Tim23 and Tim17. The architecture, assembly, and regulation of the human TIM23 complex are poorly characterized. The human genome encodes two paralogs, TIMM17A and TIMM17B. Here, we describe an unexpected role of the ovarian cancer immunoreactive antigen domain-containing protein 1 (OCIAD1) and the prohibitin complex in the biogenesis of human TIM23. Prohibitins were required to stabilize both the TIMM17A- and TIMM17B-containing variants of the translocase. Interestingly, OCIAD1 assembled with the prohibitin complex to protect the TIMM17A variant from degradation by the YME1L protease. The expression of OCIAD1 was in turn regulated by the status of the TIM23 complex. We postulate that OCIAD1 together with prohibitins constitute a regulatory axis that differentially regulates variants of human TIM23.

01 Aug 2024·Poultry Science

Comparative genome-wide association study on body weight in Chinese native ducks using four models

Article

Author: Li, Shiwei ; Zhang, Yuchen ; Wang, Sike ; Yu, Minli ; Yu, Debing ; He, Zongliang ; Lu, Yinglin ; Wu, Guansuo ; Jia, Chao

The Jinling White duck represents a newly developed breed characterized by a rapid growth rate and a superior meat quality, offering significant economic value and research potential; however, the genetic basis underlying their body weight traits remains less understood. Here, we performed whole-genome resequencing for 201 diverse Jinling White male ducks and conducted population genomic analyses, suggesting a rich genetic diversity within the Jinling White duck population. Equipped with our genomic resources, we applied genome-wide association analysis for body weight on birth (BWB), body weight on 1 wk (BW1), body weight on 3 wk (BW3), body weight on 5 wk (BW5) and body weight on 7 wk (BW7) using 4 statistical models. Comparative studies indicated that factored spectrally transformed linear mixed models (FaST-LMM) demonstrated the most superior efficiency, yielding more results with the minimal false positives. We discovered that PUS7, FBXO11, FOXN2, MSH6, and SLC4A4 were associated with BWB. RAG2, and TMEFF2 were candidate genes for BW1, and STARD13, Klotho, ZAR1L are likely candidates for BW3 and BW5. PLXNC1, ATP1A1, CD58, FRYL, OCIAD1, and OCIAD2 were linked to BW7. These findings provide a genetic reference for the selection and breeding of Jinling White ducks, while also deepened our understanding of Growth and development phenotypic in ducks.

01 Apr 2022·Aging CellQ1 · BIOLOGY

Organelle dysfunction upon asrij depletion causes aging‐like changes in mouse hematopoietic stem cells

Q1 · BIOLOGY

ArticleOA

Author: Inamdar, Maneesha S. ; Kamat, Kajal ; Sinha, Alice ; Sinha, Saloni ; Dongre, Prathamesh

AbstractAging of the blood system is characterized by increased hematopoietic stem cells (HSCs) and myeloid‐biased differentiation leading to higher propensity for hematological malignancies. Unraveling cell‐intrinsic mechanisms regulating HSC aging could aid reversal or slowing of aging. Asrij/OCIAD1 is an evolutionarily conserved regulator of hematopoiesis and governs mitochondrial, endosomal, and proteasomal function in mammalian stem cells. Asrij deletion in mice causes loss of HSC quiescence, myeloid skewing, reduced p53 and increased DNA damage, features attributed to aged HSCs. Mechanistically, Asrij controls p53 ubiquitination and degradation and AKT/STAT5 activation. Asrij localizes to endosomes and mitochondria. As decline in organelle structure and function are common hallmarks of aging, we asked whether Asrij regulates organelle function in aged HSCs. We find that chronologically aged wild‐type (WT) HSCs had reduced Asrij levels. Expectedly, young asrij KO mice had reduced AcH4K16 levels; however, transcriptome analysis of KO HSCs showed a modest overlap of gene expression with aged WT HSCs. Further, analysis of organelle structure and function in asrij KO mice revealed significant changes, namely damaged mitochondria, elevated ROS; impaired endosomal trafficking seen by increased cleaved Notch1, reduced Rab5; and reduced 26S proteasome activity. Pharmacological correction of mitochondrial and proteasome activity in asrij KO mice restored HSC and myeloid cell frequencies. Furthermore, lysophosphatidic acid‐induced Asrij upregulation in aged WT mice rescued mitochondrial and proteasome activity and restored HSC frequency. Our results highlight a new role for Asrij in preventing HSC aging by regulating organelle homeostasis and will help decipher organelle dynamics in HSC longevity.

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OCIAD1

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