+ |
PRKCB | down-regulates activity
phosphorylation
|
MFN1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273826 |
Ser86 |
AFFGRTSsGKSSVIN |
in vitro |
|
pmid |
sentence |
30659190 |
Here we report that βIIPKC accumulates on the mitochondrial outer membrane and phosphorylates mitofusin 1 (Mfn1) at serine 86. Mfn1 phosphorylation results in partial loss of its GTPase activity and in a buildup of fragmented and dysfunctional mitochondria in heart failure. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
ERK1/2 | up-regulates activity
phosphorylation
|
MFN1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274134 |
Thr562 |
LPRSLASTPTAPTTP |
Mus musculus |
MEF Cell |
pmid |
sentence |
25801171 |
Finally, in Mfn1 -/- cells re-expressing the MFN1 T562A mutant, phosphorylation was undetectable even in the presence of EGF. Taken together, these data indicate that ERK phosphorylates MFN1 at T562. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
PINK1 | down-regulates quantity
ubiquitination
|
MFN1 |
0.687 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274135 |
|
|
Homo sapiens |
SH-SY5Y Cell |
pmid |
sentence |
20871098 |
Ubiquitination of MFN-1 or MFN-2 was induced in untransfected cells and cells transfected with control siRNA. However, ubiquitination of MFN-1 and MFN-2 was significantly reduced when treated with either PINK1 siRNA combination. These results suggest that PINK1 is required for the ubiquitination of MFN-1 and MFN-2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AMFR | down-regulates quantity by destabilization
polyubiquitination
|
MFN1 |
0.315 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272886 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
23427266 |
Gp78 induces ubiquitylation and proteasomal degradation of Mfn1 and Mfn2. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
MARCHF5 | down-regulates quantity by destabilization
ubiquitination
|
MFN1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274133 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
20103533 |
MARCH5, a mitochondrial E3 ubiquitin ligase, has been identified as a molecule that binds mitochondrial fission 1 protein (hFis1), dynamin-related protein 1 (Drp1) and mitofusin 2 (Mfn2), key proteins in the control of mitochondrial fission and fusion.|Notably, a significant increase in Mfn1 level, but not Mfn2, Drp1 or hFis1 levels, was observed in MARCH5-depleted cells, indicating that Mfn1 is a major ubiquitylation substrate. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272981 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
20103533 |
MARCH5, a mitochondrial E3 ubiquitin ligase, has been identified as a molecule that binds mitochondrial fission 1 protein (hFis1), dynamin-related protein 1 (Drp1) and mitofusin 2 (Mfn2), key proteins in the control of mitochondrial fission and fusion.|Notably, a significant increase in Mfn1 level, but not Mfn2, Drp1 or hFis1 levels, was observed in MARCH5-depleted cells, indicating that Mfn1 is a major ubiquitylation substrate. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PRKN | down-regulates quantity
ubiquitination
|
MFN1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272779 |
|
|
Homo sapiens |
SH-SY5Y Cell |
pmid |
sentence |
20871098 |
Parkin and PINK1 are required for ubiquitination of MFN-1 and MFN-2. Decreases in MFN-1 and MFN-2 protein levels seen at later timepoints are difficult to interpret as it is unclear whether this is due to degradation by the proteasome and/or loss of whole mitochondria by mitophagy. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MFN1 | up-regulates
|
Mitochondrial_fusion |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272984 |
|
|
Homo sapiens |
|
pmid |
sentence |
25486875 |
OPA1, MFN1 and MFN2 are essential mediators of the sequential fusion of the outer and inner membranes of adjacent mitochondria |
|
Publications: |
1 |
Organism: |
Homo Sapiens |