Nuclear localization of the actin regulatory protein palladin in sertoli cells

Niedenberger, Bryan A.; Chappell, Vesna K.; Kaye, Evelyn P.; Renegar, Randall H.; Geyer, Christopher B.

doi:10.1002/mrd.22174

Cited by 12 publications

(21 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We previously showed that PALLD relocates from the cytoplasm to nuclei of Sertoli cells as they undergo terminal differentiation (Niedenberger et al 2013). This predominant nuclear localization was also indicated in a report published at the same time (see Fig.…”

Section: Introductionmentioning

confidence: 49%

“…1B, Supplementary Figure S2A, see section on supplementary data given at the end of this article), but was mostly nuclear in Sertoli cells isolated from 18 dpp mice (Fig. 1C, Supplementary Figure S2B), as was seen in vivo (Niedenberger et al 2013). It was previously shown that Sertoli cell morphology and cytoskeletal organization were modified in vitro by the addition of serum to culture media (Hutson et al 1980).…”

Section: Palld Localization Is Dynamic In Primary Sertoli Cellsmentioning

confidence: 87%

“…Fifteen microgram of protein were separated on a 10% SDSpolyacrylamide gel before immunoblot analysis using standard methods as described previously (Niedenberger et al 2013). The gels were blotted onto PVDF membranes and blocked in 5% nonfat milk in PBS-T.…”

Section: Immunoblot Analysismentioning

confidence: 99%

“…Immunohistochemistry (IHC) was carried out on 5 mm sections as described previously (Niedenberger et al 2013). Blocking and antibody dilutions were done in 0.05 M Tris-HCl, 0.15 M NaCl, 0.02% Triton-X-100C1% BSA, pH 7.6.…”

Section: Immunohistochemistrymentioning

confidence: 99%

“…The frozen sections were prepared as described previously (Niedenberger et al 2013) from mouse testes. PBSC0.1% Triton X-100 containing 3% BSA of pH 7.3 was used for both blocking and antibody dilution.…”

Section: Indirect Immunofluorescence On Frozen Sectionsmentioning

confidence: 99%

See 4 more Smart Citations

Actin dynamics regulate subcellular localization of the F-actin-binding protein PALLD in mouse Sertoli cells

Niedenberger¹,

Chappell²,

Otey³

et al. 2014

Reproduction

View full text Add to dashboard Cite

Sertoli cells undergo terminal differentiation at puberty to support all phases of germ cell development, which occurs in the mouse beginning in the second week of life. By w18 days postpartum (dpp), nearly all Sertoli cells have ceased proliferation. This terminal differentiation is accompanied by the development of unique and regionally concentrated filamentous actin (F-actin) structures at the basal and apical aspects of the seminiferous epithelium, and this reorganization is likely to involve the action of actin-binding proteins. Palladin (PALLD) is a widely expressed F-actin-binding and bundling protein recently shown to regulate these structures, yet it is predominantly nuclear in Sertoli cells at puberty. We found that PALLD localized within nuclei of primary Sertoli cells grown in serumfree media but relocalized to the cytoplasm upon serum stimulation. We utilized this system with in vivo relevance to Sertoli cell development to investigate mechanisms regulating nuclear localization of this F-actin-binding protein. Our results indicate that PALLD can be shuttled from the nucleus to the cytoplasm, and that this relocalization occurred following depolymerization of the F-actin cytoskeleton in response to cAMP signaling. Nuclear localization was reduced in Hpg-mutant testes, suggesting the involvement of gonadotropin signaling. We found that PALLD nuclear localization was unaffected in testis tissues from LH receptor and androgen receptor-mutant mice. However, PALLD nuclear localization was reduced in the testes of FSH receptor-mutant mice, suggesting that FSH signaling during Sertoli cell maturation regulates this subcellular localization.

show abstract

Section: Introductionmentioning

confidence: 49%

Section: Palld Localization Is Dynamic In Primary Sertoli Cellsmentioning

confidence: 87%

Section: Immunoblot Analysismentioning

confidence: 99%

Section: Immunohistochemistrymentioning

confidence: 99%

Section: Indirect Immunofluorescence On Frozen Sectionsmentioning

confidence: 99%

See 3 more Smart Citations

Actin dynamics regulate subcellular localization of the F-actin-binding protein PALLD in mouse Sertoli cells

Niedenberger¹,

Chappell²,

Otey³

et al. 2014

Reproduction

View full text Add to dashboard Cite

show abstract

Palladin expression is a conserved characteristic of the desmoplastic tumor microenvironment and contributes to altered gene expression

et al. 2015

View full text Add to dashboard Cite

The stroma surrounding solid tumors contributes in complex ways to tumor progression. Cancer-associated fibroblasts (CAFs) are the predominant cell type in the tumor stroma. Previous studies have shown that the actin-binding protein palladin is highly expressed in the stroma of pancreas tumors, but the interpretation of these results is complicated by the fact that palladin exists as multiple isoforms. In the current study, the expression and localization of palladin isoform 4 was examined in normal specimens and adenocarcinomas of human pancreas, lung, colon, and stomach samples. Immunohistochemistry with isoform-selective antibodies revealed that expression of palladin isoform 4 was higher in adenocarcinomas versus normal tissues, and highest in CAFs. Immunohistochemistry staining revealed that palladin was present in both the cytoplasm and the nucleus of CAFs, and this was confirmed using immunofluorescence staining and subcellular fractionation of a pancreatic CAF cell line. To investigate the functional significance of nuclear palladin, RNA Seq analysis of palladin knockdown CAFs versus control CAFs was performed, and the results showed that palladin regulates the expression of genes involved in the biosynthesis and assembly of collagen, and organization of the extracellular matrix. These results suggested that palladin isoform 4 may play a conserved role in establishing the phenotype of CAFs in multiple tumor types.

show abstract

Exploring the potential role of palladin in modulating human CAF/ECM functional units

Dolskii,

Alcantara dos Santos,

Andrake

et al. 2024

Cytoskeleton

View full text Add to dashboard Cite

Fibroblasts, crucial for maintaining tissue homeostasis, significantly shape the tumor microenvironment (TME). In pancreatic cancer, a highly aggressive malignancy, cancer‐associated fibroblast (CAF)/extracellular matrix (ECM) units dominate the TME, influencing tumor initiation, progression, and treatment responses. Palladin, an actin‐associated protein, is vital for fibroblast structural integrity and activation, playing a key role in CAF/ECM functionality. Palladin interacts with cytoskeletal proteins such as alpha‐actinin (α‐Act) and can therefore regulate other proteins like syndecans, modulating cytoskeletal features, cell adhesion, integrin recycling, and signaling. In this review, we propose that targeting the palladin/α‐Act/syndecan interaction network could modulate CAF/ECM units, potentially shifting the TME from a tumor‐promoting to a tumor‐suppressive state. In silico data and reported studies to suggest that stabilizing palladin‐α‐Act interactions, via excess palladin, influences syndecan functions; potentially modulating integrin endocytosis via syndecan engagement with protein kinase C alpha as opposed to syndecan binding to α‐Act. This mechanism can then affect the distribution of active α5β1‐integrin between the plasma membrane and known intracellular vesicular compartments, thereby influencing the tumor‐suppressive versus tumor‐promoting functions of CAF/ECM units. Understanding these interactions offers likely future therapeutic avenues for stroma normalization in pancreatic and other cancers, aiming to inhibit tumor progression and improve future treatment outcomes.

show abstract

Nuclear localization of the actin regulatory protein palladin in sertoli cells

Cited by 12 publications

References 41 publications

Actin dynamics regulate subcellular localization of the F-actin-binding protein PALLD in mouse Sertoli cells

Actin dynamics regulate subcellular localization of the F-actin-binding protein PALLD in mouse Sertoli cells

Palladin expression is a conserved characteristic of the desmoplastic tumor microenvironment and contributes to altered gene expression

Exploring the potential role of palladin in modulating human CAF/ECM functional units

Contact Info

Product

Resources

About