| + |
ITGA6 | up-regulates activity 
binding
|
PMP22 |
0.352 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251895 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 16436605 |
PMP22 is in a complex with α6β4 integrin and laminin. PMP22 and β4 integrin are in a complex in a variety of cell types. The interaction with the integrins provides PMP22 with the ability to modulate the cell–ECM communications, as well as intracellular events. Signaling between the ECM and the intracellular compartment is essential for SC myelination, as well as cellular differentiation and motility, in general. The identification of PMP22 as a binding partner for an integrin signaling complex provides a major step toward understanding the role of this disease-linked molecule in the nervous system and in non-neural cell types. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ITGB4 | up-regulates activity
binding
|
PMP22 |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251896 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 16436605 |
PMP22 is in a complex with α6β4 integrin and laminin. PMP22 and β4 integrin are in a complex in a variety of cell types. The interaction with the integrins provides PMP22 with the ability to modulate the cell–ECM communications, as well as intracellular events. Signaling between the ECM and the intracellular compartment is essential for SC myelination, as well as cellular differentiation and motility, in general. The identification of PMP22 as a binding partner for an integrin signaling complex provides a major step toward understanding the role of this disease-linked molecule in the nervous system and in non-neural cell types. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PMP22 | up-regulates quantity by expression 
transcriptional regulation
|
ITGA6 |
0.352 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251897 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21518455 |
Peripheral myelin protein-22 (PMP22) modulates alpha 6 integrin expression in the human endometrium. Overexpression of PMP22 was sufficient to increase α6 integrin surface expression with a concominant increase in binding to the extracellular matrix laminin, while a reduction in PMP22 suppressed α6 integrin surface expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PMP22 | up-regulates activity
binding
|
MPZ |
0.599 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251898 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10212299 |
Our data provide the first direct evidence for the formation of P0–PMP22 complexes at the plasma membrane. These protein interactions probably participate in holding adjacent Schwann cell membranes together and in stabilizing myelin compaction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PMP22
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