+ |
SUN2 | form complex
binding
|
LINC complex |
0.534 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263286 |
|
|
|
|
pmid |
sentence |
24481844 |
LINC complex couples the nuclear lamina to the cytoskeleton. SUN domain proteins, SUN1 and SUN2, located at the inner nuclear membrane (INM) interact with the nuclear lamins, Lamin A/C, B1, and B2, that line the nucleoplasmic face of the INM. SUN domain proteins interact with Nesprins in the perinuclear space (PNS). Nesprins protrude from the outer nuclear membrane (ONM) and interact with the cytoskeleton, often through an intermediate binding partner. Nesprin 1 giant (g) and Nesprin 2g potentially link the NE directly to the Z-disc (Z), whereas Nesprin 1alpha and 2alpha may connect via an unknown intermediate protein. In addition, the shorter isoforms of Nesprin 1 and Nesprin 2 may localize to the INM. |
|
Publications: |
1 |
+ |
SUN2 | up-regulates activity
binding
|
RAB5A |
0.429 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261309 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10818110 |
Rab5ip represents a novel rab5 interacting protein that may function on endocytic vesicles as a receptor for rab5-GDP and participate in the activation of rab5 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LMNA | up-regulates activity
relocalization
|
SUN2 |
0.643 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261310 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
16380439 |
In the case of Sun2, there is some evidence that A-type lamins might contribute to Sun2 localization in the INM. We report that an interaction between subunits of the HOPS complex and the ERM (ezrin, radixin, moesin) proteins is required for the delivery of EGF receptor (EGFR) to lysosomes. Inhibiting either ERM proteins or the HOPS complex leads to the accumulation of the EGFR into early endosomes, delaying its degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |