Patterns of spectrin expression in B-cell lymphomas: loss of spectrin isoforms is associated with nodule-forming and germinal center-related lymphomas

Gorman, Eric; Chen, Lugen; Albanese, Joseph; Ratech, Howard

doi:10.1038/modpathol.3800962

Cited by 13 publications

(16 citation statements)

References 33 publications

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“…Interaction of Btk with multiple components of the cytoskeleton is quite intriguing and provides a mechanism for how Btk participates in signaling processes at various subcellular locations. Another Btk interactor identified in this study, spectrin, which also has a PH domain required for membrane anchoring, has been shown to play a key role in cytoskeletal signaling during B cell diseases 33. Previous studies had demonstrated global changes in glycolytic enzyme (including GAPDH) levels by microarray during the process of T helper cell development,34 although the mechanism was unclear.…”

Section: Discussionmentioning

confidence: 75%

Highly efficient purification of protein complexes from mammalian cells using a novel streptavidin‐binding peptide and hexahistidine tandem tag system: Application to Bruton's tyrosine kinase

Franklin

Zhang

et al. 2010

Protein Science

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Tandem affinity purification (TAP) is a generic approach for the purification of protein complexes. The key advantage of TAP is the engineering of dual affinity tags that, when attached to the protein of interest, allow purification of the target protein along with its binding partners through two consecutive purification steps. The tandem tag used in the original method consists of two IgG-binding units of protein A from Staphylococcus aureus (ProtA) and the calmodulinbinding peptide (CBP), and it allows for recovery of 20-30% of the bait protein in yeast. When applied to higher eukaryotes, however, this classical TAP tag suffers from low yields. To improve protein recovery in systems other than yeast, we describe herein the development of a three-tag system comprised of CBP, streptavidin-binding peptide (SBP) and hexa-histidine. We illustrate the application of this approach for the purification of human Bruton's tyrosine kinase (Btk), which results in highly efficient binding and elution of bait protein in both purification steps (>50% recovery). Combined with mass spectrometry for protein identification, this TAP strategy facilitated the first nonbiased analysis of Btk interacting proteins. The high efficiency of the SBP-His 6 purification allows for efficient recovery of protein complexes formed with a target protein of interest from a small amount of starting material, enhancing the ability to detect low abundance and transient interactions in eukaryotic cell systems.

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Section: Discussionmentioning

confidence: 75%

Highly efficient purification of protein complexes from mammalian cells using a novel streptavidin‐binding peptide and hexahistidine tandem tag system: Application to Bruton's tyrosine kinase

Franklin

Zhang

et al. 2010

Protein Science

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“…Spectrins are large, cytoskeletal, and heterodimeric actin binding proteins which play a crucial role in maintaining the stability and architecture of the cells. Mutations of spectrin have been shown to impair cell adhesion, cell spreading, and metastasis …”

Section: Microfilamentsmentioning

confidence: 99%

The Emerging Role of Cytoskeletal Proteins as Reliable Biomarkers

2019

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Cytoskeletal proteins are essential building blocks of cells. More than 100 cytoskeletal and cytoskeleton‐associated proteins are known and for some, their function and regulation are understood in great detail. Apart from cell shape and support, they facilitate many processes such as intracellular signaling and transport, and cancer related processes such as proliferation, migration, and invasion. During the last decade, comparative proteomic studies have identified cytoskeletal proteins as in vitro markers for tumor progression and metastasis. Here, these results are summarized and a number of unrelated studies are highlighted, identifying the same cytoskeletal proteins as potential biomarkers. These findings might indicate that the abundance of these potential markers of tumor progression is associated with the biological outcome and are independent of the cancer origin. This correlates well with recently published results from the Cancer Genome Atlas, indicating that cancers show remarkable similarities in their analyzed molecular information, independent of their organ of origin. It is postulated that the quantification of cytoskeletal proteins in healthy tissues, tumors, in adjacent tissues, and in stroma, is a great source of molecular information, which might not only be used to classify tumors, but more importantly to predict patients’ outcome or even best treatment choices.

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“…217 One example is the observation of diminished aSpII in bone marrow samples from patients with acute myeloid leukemia. 218 Mutations in SPTAN1 have also been demonstrated to lead to early onset West syndrome, or Severe Early Infantile Epileptic Encephalopathy (EIEE5). EIEE5 is characterized by early onset seizures, brain atrophy, mental retardation, difficulties with walking, speech and vision.…”

Section: Spectrin and Human Diseasementioning

confidence: 99%

The Spectrinome: The Interactome of a Scaffold Protein Creating Nuclear and Cytoplasmic Connectivity and Function

Goodman

Johnson

Youngentob

et al. 2019

Exp Biol Med (Maywood)

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We provide a review of Spectrin isoform function in the cytoplasm, the nucleus, the cell surface, and in intracellular signaling. We then discuss the importance of Spectrin’s E2/E3 chimeric ubiquitin conjugating and ligating activity in maintaining cellular homeostasis. Finally we present spectrin isoform subunit specific human diseases. We have created the Spectrinome, from the Human Proteome, Human Reactome and Human Atlas data and demonstrated how it can be a useful tool in visualizing and understanding spectrins myriad of cellular functions. Impact statement Spectrin was for the first 12 years after its discovery thought to be found only in erythrocytes. In 1981, Goodman and colleagues 1 found that spectrin-like molecules were ubiquitously found in non-erythroid cells leading to a great multitude of publications over the next thirty eight years. The discovery of multiple spectrin isoforms found associated with every cellular compartment, and representing 2-3% of cellular protein, has brought us to today’s understanding that spectrin is a scaffolding protein, with its own E2/E3 chimeric ubiquitin conjugating ligating activity that is involved in virtually every cellular function. We cover the history, localized functions of spectrin isoforms, human diseases caused by mutations, and provide the spectrinome: a useful tool for understanding the myriad of functions for one of the most important proteins in all eukaryotic cells.

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Patterns of spectrin expression in B-cell lymphomas: loss of spectrin isoforms is associated with nodule-forming and germinal center-related lymphomas

Cited by 13 publications

References 33 publications

Highly efficient purification of protein complexes from mammalian cells using a novel streptavidin‐binding peptide and hexahistidine tandem tag system: Application to Bruton's tyrosine kinase

Highly efficient purification of protein complexes from mammalian cells using a novel streptavidin‐binding peptide and hexahistidine tandem tag system: Application to Bruton's tyrosine kinase

The Emerging Role of Cytoskeletal Proteins as Reliable Biomarkers

The Spectrinome: The Interactome of a Scaffold Protein Creating Nuclear and Cytoplasmic Connectivity and Function

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