+ |
PINK1 | up-regulates activity
phosphorylation
|
LETM1 |
0.367 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262540 |
Thr192 |
ILNGHSLtRRERRQF |
in vitro |
|
pmid |
sentence |
29123128 |
Here we demonstrate that PINK1 directly interacts with and phosphorylates LETM1 at Thr192 in vitro.|Phosphorylated LETM1 or the phospho-mimetic LETM1-T192E increase calcium release in artificial liposomes and facilitates calcium transport in intact mitochondria. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
LETM1 | up-regulates quantity
relocalization
|
potassium(1+) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262542 |
|
|
Mus musculus |
|
pmid |
sentence |
29123128 |
Others have suggested that LETM1 plays an essential role in mitochondrial K+ homeostasis by mediating the mitochondrial K+/H+ exchange |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
LETM1 | up-regulates
|
Mitochondrial respiratory chain complex III |
0.291 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262546 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
18628306 |
LETM1 knockdown obviously reduced the formation of the supercomplexes (Fig. 5C, arrowhead). Complexes I and IV failed to form, and the assembly of complex III was significantly decreased. By contrast, the assembly of complex II (succinate dehydrogenase) and complex V (ATP synthase) – which are not proton pumps – was unaffected. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BCS1L | up-regulates activity
binding
|
LETM1 |
0.477 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262543 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
18628306 |
LETM1 was co-precipitated with BCS1L and formation of the LETM1 complex depended on BCS1L levels, suggesting that BCS1L stimulates the assembly of the LETM1 complex. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LETM1 | up-regulates quantity
relocalization
|
calcium(2+) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262541 |
|
|
Mus musculus |
|
pmid |
sentence |
29123128 |
LETM1 is a mitochondrial inner membrane protein and several reports suggest that it mediates mitochondrial Ca2+ uptake and extrusion in a gradient-dependent manner |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
LETM1 | up-regulates
|
Mitochondrial respiratory chain complex IV |
0.294 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262548 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
18628306 |
LETM1 knockdown obviously reduced the formation of the supercomplexes (Fig. 5C, arrowhead). Complexes I and IV failed to form, and the assembly of complex III was significantly decreased. By contrast, the assembly of complex II (succinate dehydrogenase) and complex V (ATP synthase) – which are not proton pumps – was unaffected. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LETM1 | up-regulates
|
Mitochondrial_biogenesis |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262545 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
18628306 |
We hypothesize a working model of the function of BCS1L and LETM1 in mitochondrial biogenesis (Fig. 8E). Because BCS1L is an AAA-ATPase, the following three functions are downstream targets: (1) respiratory chain assembly, (2) mitochondrial morphology maintenance and, (3) LETM1 complex formation. BCS1L functions directly in the formation of mitochondrial tubular networks, in addition to the assembly of the supercomplexes. LETM1 has a distinct role in maintenance of mitochondrial volume and shapes, which helps – in concert with BCS1L – to achieve the efficient assembly of the respiratory chains. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LETM1 | up-regulates
|
Mitochondrial respiratory chain complex I |
0.256 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262547 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
18628306 |
LETM1 knockdown obviously reduced the formation of the supercomplexes (Fig. 5C, arrowhead). Complexes I and IV failed to form, and the assembly of complex III was significantly decreased. By contrast, the assembly of complex II (succinate dehydrogenase) and complex V (ATP synthase) – which are not proton pumps – was unaffected. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |