Palladin, Cytoskeletal Associated Protein Proteins (PALLD)

Human Palladin, Cytoskeletal Associated Protein (PALLD) interaction partners

1. Twist1 (show TWIST1 Proteins) appears to require both palladin and collagen alpha1(VI) as downstream effectors for its prometastatic effects, which could be future therapeutic targets in cancer metastasis.

2. Palladin role in the vascular smooth muscle cell differentiation and gene expression

3. stromal palladin expression is a surrogate indicator of the treatment effect after chemoradiation therapy.

4. Study identified the actin-associated protein palladin as a key node in signaling pathways that result in fibroblast activation in the increased tissue stiffness of a tumor microenvironment

5. Palladin interacts with MT1-MMP (show MMP14 Proteins) to promote tumor cell invasion in breast carcinoma.

6. palladin functions as a dynamic scaffolding protein that promotes the assembly of dorsal stress fibers by recruiting VASP (show VASP Proteins) to these structures.

7. Palladin seems to regulate podosome and invodopodia formation through Rho GTPases. [Review]

8. A model whereby palladin-activated fibroblasts facilitate stromal-dependent metastasis and outgrowth of tumorigenic epithelium.

9. results indicate that palladin phosphorylation by ERK (show EPHB2 Proteins) has an anti-migratory function, possibly by modulating interactions with molecules that regulate cell migration

10. Observations support the belief that stromal palladin assessments have clinical relevance thus validating the use of these 3D cultures to study both progressive RCC (show XRCC1 Proteins)-associated stroma and stroma-dependent mechanisms affecting tumorigenesis.

Mouse (Murine) Palladin, Cytoskeletal Associated Protein (PALLD) interaction partners

1. Study shows palladin is expressed with proper spatio-temporal pattern in the neural folds. It plays a crucial role in regulating mouse cranial neural tube closure by modulating cytoskeleton, proliferation, differentiation, apoptosis, and adhesion of neural epithelium

2. these results show a new function for PALLD as a crucial regulator of the early phase of phagocytosis by elaborating dynamic actin polymerization and depolymerization

3. Interactions with phosphatidylinositol 4,5-bisphosphate decrease the actin polymerizing activity of Ig domain 3 of palladin (Palld-Ig3).

4. The aggregation of palladin(+/-) platelets was increased in response to low levels of thrombin (show F2 Proteins), U46619, and collagen. This study also reports enhanced spreading of palladin(+/-) platelets on immobilized fibrinogen (Fg) and increased rate of clot (show TXNDC17 Proteins) retraction in platelet-rich plasma (PRP) containing palladin(+/-) platelets.

5. The inhibition of palladin in myoblasts stimulates them to exit the cell cycle and express myogenic markers at the early phases of myogenesis, but retards the formation of multinucleated myotubes via the enhanced activation of myostatin (show MSTN Proteins).

6. Suggesting that FSH (show BRD2 Proteins) signaling during Sertoli cell maturation regulates subcellular localization of palladin.

7. Palladin is required for migration behavior and differentiation potential of cultured myoblast cells.

8. High levels of palladin expression in cancer associated fibroblasts enhance their ability to remodel the extracellular matrix by regulating the activity of Cdc42 (show CDC42 Proteins).

9. 140 kDa isoform of PALLD predominates in Sertoli cells, and that it is apparently cleaved, with the C-terminus localizing to the nucleus while the N-terminus remains cytoplasmic.

10. Palladin mutations that disrupt actin binding show altered cellular distributions and morphology of actin in cells, revealing a functional requirement for the interaction between palladin and actin in vivo.