| 2013 |
SFXN4 localizes to the mitochondrial inner membrane and is required for mitochondrial respiratory homeostasis and erythropoiesis; loss-of-function mutations cause mitochondrial respiratory defects and macrocytic anemia, demonstrated by sfxn4 knockdown in zebrafish and in vitro/in vivo complementation with patient fibroblasts. |
Exome sequencing, zebrafish morpholino knockdown, in vitro and in vivo complementation studies with patient fibroblasts |
American journal of human genetics |
High |
24119684
|
| 2019 |
SFXN4 knockout reduces Fe-S cluster formation, diminishes mitochondrial respiratory chain complex stability and activity, causes a shift to glycolytic metabolism, affects the cytosolic aconitase-IRP1 switch, redistributes iron from cytosol to mitochondria, reduces ferrochelatase levels, and inhibits translation of ALAS2. |
SFXN4 knockout cell lines, Fe-S cluster activity assays, metabolic flux analysis (glycolysis vs. respiration), immunoblot for ferrochelatase, ALAS2 translation assay |
Scientific reports |
Medium |
31873120
|
| 2022 |
SFXN4 functions as a complex I assembly factor that interacts with the MCIA (Mitochondrial Complex I Assembly) complex and is specifically required for assembly of the ND2 module of mitochondrial complex I. |
Co-immunoprecipitation, complexome profiling, SFXN4 KO cell lines with complex I assembly assays, interaction studies with MCIA complex components |
Proceedings of the National Academy of Sciences of the United States of America |
High |
35333655
|
| 2022 |
SFXN4 knockdown in ovarian cancer cells inhibits Fe-S cluster biogenesis, leading to accumulation of excess iron and oxidative stress, and reduces activity of Fe-S-dependent DNA repair enzymes, thereby sensitizing cells to DNA-damaging agents and PARP inhibitors; SFXN4 knockout inhibits tumor growth in a mouse xenograft model. |
siRNA knockdown, Fe-S cluster activity assays, ROS measurements, DNA repair assays, cisplatin/PARP inhibitor sensitivity assays, mouse xenograft tumor growth experiments |
Scientific reports |
Medium |
36402786
|
| 2019 |
SFXN4 loss-of-function mutations cause complex I enzyme activity deficiency with loss of complex I subunit proteins and ultrastructural mitochondrial abnormalities, as shown in muscle tissue from a patient with bi-allelic SFXN4 mutations. |
Whole-exome sequencing, mitochondrial enzyme activity assays, immunoblot for complex I subunit proteins, electron microscopy of muscle, mRNA expression analysis |
Mitochondrion |
Medium |
31059822
|
| 2003 |
SFXN4 encodes a 305-amino acid protein with a predicted five-transmembrane-domain structure, consistent with a mitochondrial transporter, and is expressed in many tissues. |
cDNA cloning from human fetal brain library, sequence analysis, RT-PCR expression profiling, genomic mapping |
DNA sequence : the journal of DNA sequencing and mapping |
Low |
14756423
|
| 2023 |
In CLPP-deficient mouse testis, SFXN4 accumulates alongside COX15 as a complex IV metal-binding assembly factor co-accumulating with heavy metals (iron, molybdenum, cobalt, manganese), suggesting SFXN4 participates in mitochondrial metal/iron handling during complex assembly. |
Complexome profiling (complexomics), heavy metal quantification, immunoblot validation in mouse tissue |
International journal of molecular sciences |
Low |
38139332
|
| 2025 |
SFXN4 is implicated in mitochondrial iron regulation, heme biosynthesis, and iron-sulfur cluster assembly, with SFXN1 and SFXN3 specializing in serine transport while SFXN2 and SFXN4 specialize in iron-related functions; SFXNs share conserved transmembrane domains critical for substrate transport. |
Comparative genomics and literature review of family function; structural domain analysis |
Human genomics |
Low |
40542427
|