NH2-terminal processing of actin in mouse L-cells in vivo.

Rubenstein, P A; Martin, D J

doi:10.1016/s0021-9258(18)32761-3

Cited by 66 publications

(13 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Mammalian band gactin (1)(2)(3)(4) are encoded by different genes and differ substantially at the nucleotide level, but are nearly identical in their amino acid sequences, with only four homologous substitutions near their N termini. N-terminal methionine (M) in the actin sequence is removed immediately after synthesis, exposing the aspartic acid (in b-actin) or glutamic acid (in g-actin) that can undergo subsequent posttranslational modifications (5). Arginylation, posttranslational addition of arginine (R) to proteins mediated by arginyltransferase (6), affects cytoskeletal proteins (7) and regulates actin (8); however, only b-actin is posttranslationally arginylated on the N terminus in vivo (8).…”

mentioning

confidence: 99%

“…In addition to selective degradation, actin isoforms may also be selectively recognized by arginyltransferase, either via the specificity of the enzyme itself or by its spatial segregation toward one actin isoform. However, arginyltransferase has fairly poor substrate specificity (7), and it can efficiently arginylate both N-terminal Asp and Glu (19,20), found at the N terminus of band g-actin, respectively (5). Spatial segregation toward one actin isoform is also unlikely, because arginyltransferase appears to have no relevant bias in its intracellular distribution (19,20).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Differential Arginylation of Actin Isoforms Is Regulated by Coding Sequence–Dependent Degradation

Zhang

Saha

Shabalina

et al. 2010

Science

187

192

View full text Add to dashboard Cite

The mammalian cytoskeletal proteins β- and γ-actin are highly homologous, but only β-actin is N-terminally arginylated, which regulates its function. Here we examined the metabolic fate of exogenously expressed arginylated and non-arginylated actin isoforms. Arginylated γ-actin, unlike β-, was highly unstable and was selectively ubiquitinated and degraded in vivo. This instability was regulated by the differences in the coding sequence between the two actin isoforms, which conferred different translation rates. γ-actin was translated more slowly than β-actin, and this slower processing resulted in the exposure of a normally hidden lysine residue for ubiquitination, leading to the preferential degradation of γ-actin upon arginylation. This degradation mechanism, coupled to nucleotide coding sequence, may regulate protein arginylation in vivo.

show abstract

mentioning

confidence: 99%

mentioning

confidence: 99%

Differential Arginylation of Actin Isoforms Is Regulated by Coding Sequence–Dependent Degradation

Zhang

Saha

Shabalina

et al. 2010

Science

187

192

View full text Add to dashboard Cite

show abstract

“…While no other Met-APs have been described, the repertoire of proteins found in vivo with removed N-terminal Met increasingly suggests that other classes of Met-APs must exist in cells, with specificity for residues in the second position that goes beyond the limited list of those recognized by Met-AP1 and Met-AP2. For example, cytoplasmic actins are processed by removal of N-terminal Met preceding negatively charged residues (Asp or Glu), which occurs after Met acetylation ( Redman and Rubenstein, 1981 ; Rubenstein and Martin, 1983 ; Martin and Rubenstein, 1987 ; Van Damme et al, 2012 ). The enzyme mediating this removal has been biochemically enriched but never definitively identified ( Sheff and Rubenstein, 1992 ).…”

Section: N-terminal Post-translational Modificationsmentioning

confidence: 99%

Post-translational Modifications of the Protein Termini

Chen

Kashina

2021

Front. Cell Dev. Biol.

View full text Add to dashboard Cite

Post-translational modifications (PTM) involve enzyme-mediated covalent addition of functional groups to proteins during or after synthesis. These modifications greatly increase biological complexity and are responsible for orders of magnitude change between the variety of proteins encoded in the genome and the variety of their biological functions. Many of these modifications occur at the protein termini, which contain reactive amino- and carboxy-groups of the polypeptide chain and often are pre-primed through the actions of cellular machinery to expose highly reactive residues. Such modifications have been known for decades, but only a few of them have been functionally characterized. The vast majority of eukaryotic proteins are N- and C-terminally modified by acetylation, arginylation, tyrosination, lipidation, and many others. Post-translational modifications of the protein termini have been linked to different normal and disease-related processes and constitute a rapidly emerging area of biological regulation. Here we highlight recent progress in our understanding of post-translational modifications of the protein termini and outline the role that these modifications play in vivo.

show abstract

“…Actin isoforms undergo a unique maturation process at the N‐terminus during and after synthesis (Figure 3b; Redman & Rubenstein, 1981; Rubenstein & Martin, 1983). For non‐muscle β‐actin and γ‐actin, the initiator Met is co‐translationally acetylated by NatB, followed by removal of the acetylated Met1 by an aminopeptidase that has still not been identified (Van Damme et al, 2012).…”

Section: Actinmentioning

confidence: 99%

Posttranslational modifications of the cytoskeleton

MacTaggart

Kashina

2021

Cytoskeleton

View full text Add to dashboard Cite

The cytoskeleton plays important roles in many essential processes at the cellular and organismal levels, including cell migration and motility, cell division, and the establishment and maintenance of cell and tissue architecture. In order to facilitate these varied functions, the main cytoskeletal components—microtubules, actin filaments, and intermediate filaments—must form highly diverse intracellular arrays in different subcellular areas and cell types. The question of how this diversity is conferred has been the focus of research for decades. One key mechanism is the addition of posttranslational modifications (PTMs) to the major cytoskeletal proteins. This posttranslational addition of various chemical groups dramatically increases the complexity of the cytoskeletal proteome and helps facilitate major global and local cytoskeletal functions. Cytoskeletal proteins undergo many PTMs, most of which are not well understood. Recent technological advances in proteomics and cell biology have allowed for the in‐depth study of individual PTMs and their functions in the cytoskeleton. Here, we provide an overview of the major PTMs that occur on the main structural components of the three cytoskeletal systems—tubulin, actin, and intermediate filament proteins—and highlight the cellular function of these modifications.

show abstract

NH2-terminal processing of actin in mouse L-cells in vivo.

Cited by 66 publications

References 26 publications

Differential Arginylation of Actin Isoforms Is Regulated by Coding Sequence–Dependent Degradation

Differential Arginylation of Actin Isoforms Is Regulated by Coding Sequence–Dependent Degradation

Post-translational Modifications of the Protein Termini

Posttranslational modifications of the cytoskeleton

Contact Info

Product

Resources

About