A PPP-type pseudophosphatase is required for the maintenance of basal complex integrity in Plasmodium falciparum

Alexander A Morano1,2, Rachel M Rudlaff1,2, Jeffrey D Dvorin3,4

  • 1Biological and Biomedical Sciences, Harvard Medical School, Boston, MA, 02115, USA.

PubMed

Insights

Researchers identified a new protein, PfPPP8, crucial for maintaining the basal complex during Plasmodium falciparum asexual reproduction. This discovery reveals the complex

Area of Science:

  • Cell Biology
  • Parasitology
  • Molecular Biology

Background:

  • Plasmodium falciparum replicates asexually through schizogony, a process involving the formation of multiple daughter cells within a parent cell.
  • The basal complex, a contractile ring structure, is essential for the proper separation of daughter cells during schizogony in P. falciparum.
  • Understanding the molecular components and dynamics of the basal complex is critical for comprehending P. falciparum's replication cycle.

Purpose of the Study:

  • To identify and characterize novel proteins involved in the maintenance and function of the Plasmodium falciparum basal complex.
  • To elucidate the role of PfPPP8 in basal complex integrity and expansion during schizogony.
  • To investigate the broader implications of these findings for Apicomplexan parasite biology.

Main Methods:

  • Utilized multiple microscopy techniques to visualize and analyze the basal complex.
  • Employed co-immunoprecipitation to identify novel interacting proteins within the basal complex.
  • Characterized the temporal localization of identified proteins using advanced imaging methods.

Main Results:

  • Identified PfPPP8 as a novel basal complex protein essential for its uniform expansion and integrity.
  • Characterized PfPPP8 as the first member of a new pseudophosphatase family with homologs in other Apicomplexan parasites.
  • Discovered two additional novel basal complex proteins and detailed the distinct temporal localizations of PfPPP8 and these new proteins.

Conclusions:

  • PfPPP8 plays a critical role in basal complex maintenance and parasite segmentation.
  • The P. falciparum basal complex is a dynamic structure with proteins exhibiting unique temporal localization patterns.
  • The identification of a new pseudophosphatase family opens avenues for further research into Apicomplexan parasite biology.

Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
13.2K
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
8.6K
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
4.9K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
5.8K
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
50.6K
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
4.4K