ArticleCell cycle (Georgetown, Tex.)2014
Identification of the nuclear localization signal of SALL4B, a stem cell transcription factor.
Article in Cell cycle (Georgetown, Tex.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- ADT increases prostate cancer cell invasion via altering AR/SALL4/SOX2-OCT4 stem cell signaling.Cell biology and toxicology · 2025Article
- Cytoplasmic SALL4-A isoform expression as a diagnostic marker of less aggressive tumor behavior in gastric cancer.World journal of surgical oncology · 2025Article
- SALL4 in gastrointestinal tract cancers: upstream and downstream regulatory mechanisms.Molecular medicine (Cambridge, Mass.) · 2024Review
- Review
- Defining the Pluripotent Marker Genes for Identification of Teleost Fish Cell Pluripotency During Reprogramming.Frontiers in genetics · 2022Article
- Expression and clinical value of SALL4 in renal cell carcinomas.Molecular medicine reports · 2020Article
- Spalt-like transcription factor 4 expression in oral epithelial dysplasia and oral squamous cell carcinoma: An immunohistochemical appraisal.Journal of carcinogenesis · 2020Article
- Sal-like 4 protein levels in breast cancer cells are post-translationally down-regulated by tripartite motif-containing 21.The Journal of biological chemistry · 2018Article
- Review
- Nuclear localization of SALL4: a stemness transcription factor.Cell cycle (Georgetown, Tex.) · 2014Article
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Authors and funding
7 authors at 5 institutions in 4 countries.
Funding
Abstract
SALL4B plays a critical role in maintaining the pluripotency of embryonic stem cells and hematopoietic stem cells. SALL4B primarily functions as a transcription factor, and, thus, its nuclear localization is paramount to its biological activities. To understand the structural basis by which SALL4B was transported and retained in the nucleus, we made a series of SALL4B constructs with deletions or point mutations. We found that K64R mutation resulted in a random distribution of SALL4B within the cell. An analysis of neighboring amino acid sequences revealed that (64)KRLR (67) in SALL4B matches exactly with the canonical nuclear localization signal (K-K/R-x-K/R). SALL4B fragment (a.a. 50-109) that contained KRLR was sufficient for targeting GFP-tagged SALL4B to the nucleus, whereas K64R mutation led to a random distribution of GFP-SALL4B signal within the cell. We further demonstrated that the nuclear localization was essential for transactivating luciferase reporter gene driven by OCT4 promoter, a known transcriptional target of SALL4B. Therefore, our study identifies the KRLR sequence as a bona fide nuclear localization signal for SALL4B.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.