Multifunctional protein 4.1R regulates the asymmetric segregation of Numb during terminal erythroid maturation

Huang, Shu-Ching; Vu, Long V.; Yu, Faye; Nguyen, Dan Trong; Benz, Edward J.

doi:10.1016/j.jbc.2021.101051

Cited by 6 publications

(4 citation statements)

References 76 publications

(103 reference statements)

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“…In adult brain and pituitary gland, immune and hematopoietic system, on average both exon 9 and exon 3 inclusion level is lower than 25%, suggesting that the p65 (Ex9sk & Ex3sk) Numb isoform is predominantly expressed (Table 1). These observations are consistent with previously observed changes in both exon 9 and exon 3 inclusion during development measured using RT-PCR or protein expression: rat and human brain (Verdi, Bashirullah et al 1999, Dooley, James et al 2003, Bani-Yaghoub, Kubu et al 2007, mouse pituitary gland (Moran, Goldberg et al 2011), rat auditory epithelium (Gao, Chi et al 2011), and human and mouse erythroid cells (Huang, Vu et al 2021).…”

Section: Resultssupporting

confidence: 93%

Pan tissue analysis of humanNUMBalternative splicing

Zhang,

McGlade

2023

Preprint

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Alternative splicing (AS) of pre-mRNA generates multiple protein isoforms from a single gene. It is developmentally regulated and mis-regulation is associated with many diseases. Previous studies that examined AS of the cell fate determinantNUMBdemonstrated that it undergoes a regulated switch in the inclusion of protein coding exons 3 and 9 during rodent development and the differentiation of human cell lines. Here we extend this work by comparing exon 9 and exon 3 inclusion levels of the humanNUMBgene across different normal human tissues by analysis of RNA sequencing data deposited in the Genotype-Tissue Expression (GTEx) and the Vertebrate Alternative Splicing and Transcription (VastDB) databases. Our results support earlier studies and reveal specific Numb isoform expression patterns in previously unexamined tissue and cell types, suggesting that Numb isoform expression is regulated in the normal development of a broad range of tissue types throughout the body.

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Section: Resultssupporting

confidence: 93%

Pan tissue analysis of humanNUMBalternative splicing

Zhang,

McGlade

2023

Preprint

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“…Recently, Huang et al suggested that 4.1R regulates the asymmetric segregation of the Notch signaling regulatory protein Numb during terminal erythroid maturation. They also identified a critical role for 4.1R in mediating erythropoiesis [25].…”

Section: Cell Divisionmentioning

confidence: 99%

“…Consequently, these depletions notably increase the proportion of symmetric distribution of Numb. Knockdown of 4.1R reduces the size of Numb in the daughter cells and enhances Notch signaling, directly promoting cell proliferation and delaying cell maturation [25].…”

Section: Cell Fate Regulationmentioning

confidence: 99%

Cytoskeletal Protein 4.1R in Health and Diseases

Liu,

Ding,

Liu

et al. 2024

Biomolecules

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The protein 4.1R is an essential component of the erythrocyte membrane skeleton, serving as a key structural element and contributing to the regulation of the membrane’s physical properties, including mechanical stability and deformability, through its interaction with spectrin–actin. Recent research has uncovered additional roles of 4.1R beyond its function as a linker between the plasma membrane and the membrane skeleton. It has been found to play a crucial role in various biological processes, such as cell fate determination, cell cycle regulation, cell proliferation, and cell motility. Additionally, 4.1R has been implicated in cancer, with numerous studies demonstrating its potential as a diagnostic and prognostic biomarker for tumors. In this review, we provide an updated overview of the gene and protein structure of 4.1R, as well as its cellular functions in both physiological and pathological contexts.

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“…Thus, rather than simply being a regulatory or even a structural protein, we posit that BAG3 serves as a universal glue that selectively localizes proteins to specific cellular domains as well as to partner proteins [ 12 ]. While not common, there are examples of this type of protein multi-tasking: the multi-functional protein 4.1R being a good example [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

BAG3: Nature’s Quintessential Multi-Functional Protein Functions as a Ubiquitous Intra-Cellular Glue

Brenner

Choudhary

McCormick

et al. 2023

Cells

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BAG3 is a 575 amino acid protein that is found throughout the animal kingdom and homologs have been identified in plants. The protein is expressed ubiquitously but is most prominent in cardiac muscle, skeletal muscle, the brain and in many cancers. We describe BAG3 as a quintessential multi-functional protein. It supports autophagy of both misfolded proteins and damaged organelles, inhibits apoptosis, maintains the homeostasis of the mitochondria, and facilitates excitation contraction coupling through the L-type calcium channel and the beta-adrenergic receptor. High levels of BAG3 are associated with insensitivity to chemotherapy in malignant cells whereas both loss of function and gain of function variants are associated with cardiomyopathy.

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Multifunctional protein 4.1R regulates the asymmetric segregation of Numb during terminal erythroid maturation

Cited by 6 publications

References 76 publications

Pan tissue analysis of humanNUMBalternative splicing

Pan tissue analysis of humanNUMBalternative splicing

Cytoskeletal Protein 4.1R in Health and Diseases

BAG3: Nature’s Quintessential Multi-Functional Protein Functions as a Ubiquitous Intra-Cellular Glue

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