Palladin, Cytoskeletal Associated Protein Proteine (PALLD)

Human Palladin, Cytoskeletal Associated Protein (PALLD) Interaktionspartner

1. Collectively, our results demonstrate that palladin can functionally replace the Arp2/3 complex during bacterial actin-based cellular entry and intracellular motility of Listeria monocytogenes.

2. Twist1 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.

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

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

5. 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

6. Palladin interacts with MT1-MMP to promote tumor cell invasion in breast carcinoma.

7. palladin functions as a dynamic scaffolding protein that promotes the assembly of dorsal stress fibers by recruiting VASP to these structures.

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

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

10. results indicate that palladin phosphorylation by ERK has an anti-migratory function, possibly by modulating interactions with molecules that regulate cell migration

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

12. Palladin may identify primary pancreatic endocrine neoplasms with a propensity to metastasize to the liver

13. these results suggested that palladin played a specific role in modulating the subcellular localization of the cytoplasmic ILKAP and promoting the ILKAP-induced apoptosis.

14. The A-allele of PALLD rs7439293 was not associated with progressive carotid atherosclerosis

15. upregulation of 85-90 kDa palladin isoform may play a role in the establishment of the tumor-associated fibroblasts phenotype, and thus in the formation of a desmoplastic tumor microenvironment

16. Akt signaling regulates the stability of palladin

17. Palladin is an integral component of adherens junctions and plays a role in the localization of E-cadherin to the junctions. The loss of palladin may be an integral part of EMT, an early step in the metastatic spread of colon carcinoma.

18. Akt1 phosphorylates palladin, inducing cytoskeletal reorganization and inhibiting the migration of breast cancer cells.

19. Quantitative analysis of erythrocyte membrane proteins revealed decrease in palladin from patients with homozygous and heterozygous forms of beta-thalassemia.

20. Our results suggest that palladin may play an important role in recruiting profilin to sites of actin dynamics.

Mouse (Murine) Palladin, Cytoskeletal Associated Protein (PALLD) Interaktionspartner

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, U46619, and collagen. This study also reports enhanced spreading of palladin(+/-) platelets on immobilized fibrinogen (Fg) and increased rate of clot 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.

6. Suggesting that FSH 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.

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.

11. upregulation of 85-90 kDa palladin isoform may play a role in the establishment of the tumor-associated fibroblasts phenotype, and thus in the formation of a desmoplastic tumor microenvironment

12. Actin associated protein palladin is important for the early smooth muscle cell differentiation.

13. palladin is dispensable for normal neurite outgrowth in mice

14. The actin-associated protein palladin may play an important role in recruiting VASP to sites of actin filament growth, anchorage, and crosslinking.

15. We propose that palladin is required for the initiation of neural tube closure and provides an important new candidate that may be implicated in the etiology of human NTDs.

16. Here, we demonstrate that palladin is a binding partner for profilin, interacting with profilin via a poly proline-containing sequence in the amino-terminal half of palladin.

17. palladin is crucial for definitive erythropoiesis and erythroblastic island formation

18. expression analysis of the murine palladin isoforms

19. Palladin is essential for expression of the full complement of contractile proteins necessary for optimal force development of smooth muscle cells derived from embryoid bodies

20. results indicate that alpha-actinin, CLP36 and palladin form a protein complex and contribute to regulation of the actin cytoskeleton