Reconstituting the actin cytoskeleton at or near surfaces in vitro

Cáceres, Rodrigo; Abou-Ghali, Majdouline; Plastino, Julie

doi:10.1016/j.bbamcr.2015.07.021

Cited by 15 publications

(7 citation statements)

References 114 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…S2), whereas in the absence of CP, no comets were observable (see Ref. 26 and references therein). Unexpectedly adding VASP to the assay instead of CP produced robust actin comet formation and bead motility (Fig.…”

Section: Resultsmentioning

confidence: 99%

Capping protein is dispensable for polarized actin network growth and actin-based motility

Abou-Ghali

Kusters

Körber

et al. 2020

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Heterodimeric capping protein (CP) binds the rapidly growing barbed ends of actin filaments and prevents the addition (or loss) of subunits. Capping activity is generally considered to be essential for actin-based motility induced by Arp2/3 complex nucleation. By stopping barbed end growth, CP favors nucleation of daughter filaments at the functionalized surface where the Arp2/3 complex is activated, thus creating polarized network growth, which is necessary for movement. However, here using an in vitro assay where Arp2/3 complex-based actin polymerization is induced on bead surfaces in the absence of CP, we produce robust polarized actin growth and motility. This is achieved either by adding the actin polymerase Ena/VASP or by boosting Arp2/3 complex activity at the surface. Another actin polymerase, the formin FMNL2, cannot substitute for CP, showing that polymerase activity alone is not enough to override the need for CP. Interfering with the polymerase activity of Ena/VASP, its surface recruitment or its bundling activity all reduce Ena/VASP’s ability to maintain polarized network growth in the absence of CP. Taken together, our findings show that CP is dispensable for polarized actin growth and motility in situations where surface-directed polymerization is favored by whatever means over the growth of barbed ends in the network.

show abstract

Section: Resultsmentioning

confidence: 99%

Capping protein is dispensable for polarized actin network growth and actin-based motility

Abou-Ghali

Kusters

Körber

et al. 2020

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…The organization of these filaments within the cell is the main determinant of the cell's shape. Actin polymerization is a very dynamic process that has been widely studied in eukaryotes ; it is involved in several cellular functions, including intracellular trafficking, endocytosis and morphology maintenance. Actin homologs among eukaryotes share high similarity both in their structure and in their ability to polymerize into filaments .…”

Section: Cytoskeleton Elementsmentioning

confidence: 99%

Membrane remodeling and organization: Elements common to prokaryotes and eukaryotes

Vega-Cabrera

Pardo-López

2017

IUBMB Life

View full text Add to dashboard Cite

Membrane remodeling processes in eukaryotes, such as those involved in endocytosis and intracellular trafficking, are mediated by a large number of structural, accessory and regulatory proteins. These processes occur in all cell types, enabling the exchange of signals and/or nutrients with the external medium and with neighboring cells; likewise, they are required for the intracellular trafficking of various cargo molecules between organelles, as well as the recycling of these structures. Recent studies have demonstrated that some elements of the molecular machinery involved in regulating and mediating endocytosis in eukaryotic cells are also present in some bacteria, where they participate in processes such as cell division, sporulation and signal transduction. However, the mechanism whereby this prokaryotic machinery carries out such functions has barely begun to be elucidated. This review summarizes recent information about the cytoskeletal and membrane-organizing proteins for which bacterial homologs have been identified; given their known functions, they may be considered to be part of an ancestral membrane organization system that first emerged in prokaryotes and which further evolved into the more complex regulatory networks operating in eukaryotes. © 2017 IUBMB Life, 69(2):55-62, 2017.

show abstract

“…The Arp2/3 complex, when it is working in concert with bundling proteins such as palladin, Eps8, ezrin, and plastin, confer plasticity to the actin-based cytoskeleton, necessary for cell motility, cell division, development, and also endocytic vesicle-mediated protein trafficking (Blanchoin, et al 2014, Caceres, et al 2015, Coticchio, et al 2015, Dawson, et al 2006). As depicted in Figure 2, Arp3 has been shown to work in coordination with the actin bundling proteins so that these two ABPs provide an effective mechanism to facilitate the transport of preleptotene spermatocytes.…”

Section: Regulation Of Btb Actin-based Cytoskeleton By Abps and Prmentioning

confidence: 99%

Regulation of blood–testis barrier by actin binding proteins and protein kinases

Li¹,

Tang²,

Cheng³

2016

Reproduction

View full text Add to dashboard Cite

The blood-testis barrier (BTB) is an important ultrastructure in the testis since the onset of spermatogenesis coincides with the establishment of a functional barrier in rodents and humans. It is also noted that a delay in the assembly of a functional BTB following treatment of neonatal rats with drugs such as diethylstilbestrol or adjudin also delays the first wave of spermiation. While the BTB is one of the tightest blood-tissue barriers, it undergoes extensive remodeling, in particular at stage VIII of the epithelial cycle to facilitate the transport of preleptotene spermatocytes connected in clones across the immunological barrier. Without this timely transport of preleptotene spermatocytes derived from type B spermatogonia, meiosis will be arrested, causing aspermatogenesis. Yet the biology and regulation of the BTB remains largely unexplored since the morphological studies in the 1970s. Recent studies, however, have shed new light on the biology of the BTB. Herein, we critically evaluate some of these findings, illustrating that the Sertoli cell BTB is regulated by actin binding proteins (ABPs), likely supported by non-receptor protein kinases, to modulate the organization of actin microfilament bundles at the site. Furthermore, microtubule (MT)-based cytoskeleton is also working in concert with the actin-based cytoskeleton to confer BTB dynamics. This timely review provides an update on the unique biology and regulation of the BTB based on the latest findings in the field, focusing on the role of ABPs and non-receptor protein kinases.

show abstract

Reconstituting the actin cytoskeleton at or near surfaces in vitro

Cited by 15 publications

References 114 publications

Capping protein is dispensable for polarized actin network growth and actin-based motility

Capping protein is dispensable for polarized actin network growth and actin-based motility

Membrane remodeling and organization: Elements common to prokaryotes and eukaryotes

Regulation of blood–testis barrier by actin binding proteins and protein kinases

Contact Info

Product

Resources

About