NDLI: An actin cytoskeleton with evolutionarily conserved functions in the absence of canonical actin-binding proteins

Content Provider	PubMed Central
Author	Paredez, Alexander R. Assaf, Zoe June Sept, David Timofejeva, Ljudmilla Dawson, Scott C. Wang, Chung-ju Rachel Cande, W. Z.
Abstract	Giardia intestinalis, a human intestinal parasite and member of what is perhaps the earliest-diverging eukaryotic lineage, contains the most divergent eukaryotic actin identified to date and is the first eukaryote known to lack all canonical actin-binding proteins (ABPs). We sought to investigate the properties and functions of the actin cytoskeleton in Giardia to determine whether Giardia actin (giActin) has reduced or conserved roles in core cellular processes. In vitro polymerization of giActin produced filaments, indicating that this divergent actin is a true filament-forming actin. We generated an anti-giActin antibody to localize giActin throughout the cell cycle. GiActin localized to the cortex, nuclei, internal axonemes, and formed C-shaped filaments along the anterior of the cell and a flagella-bundling helix. These structures were regulated with the cell cycle and in encysting cells giActin was recruited to the Golgi-like cyst wall processing vesicles. Knockdown of giActin demonstrated that giActin functions in cell morphogenesis, membrane trafficking, and cytokinesis. Additionally, Giardia contains a single G protein, giRac, which affects the Giardia actin cytoskeleton independently of known target ABPs. These results imply that there exist ancestral and perhaps conserved roles for actin in core cellular processes that are independent of canonical ABPs. Of medical significance, the divergent giActin cytoskeleton is essential and commonly used actin-disrupting drugs do not depolymerize giActin structures. Therefore, the giActin cytoskeleton is a promising drug target for treating giardiasis, as we predict drugs that interfere with the Giardia actin cytoskeleton will not affect the mammalian host.
Related Links	http://dx.doi.org/10.1073/pnas.1018593108
Starting Page	6151
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	15
Volume Number	108
Language	English
Publisher	National Academy of Sciences
Publisher Date	2011-04-12
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

An actin cytoskeleton with evolutionarily conserved functions in the absence of canonical actin-binding proteins.

Evolutionarily conserved surface residues constitute actin binding sites of tropomyosin

A Periodic Pattern of Evolutionarily Conserved Basic and Acidic Residues Constitutes the Binding Interface of Actin-Tropomyosin

An evolutionarily conserved protein binding sequence upstream of a plant light-regulated gene.

Mouse cytoplasmic polyadenylylation element binding protein: An evolutionarily conserved protein that interacts with the cytoplasmic polyadenylylation elements of c-mos mRNA

Controlling the Gate: The Functions of the Cytoskeleton in Stomatal Movement

Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity

Editorial: Evolution, Emerging Functions and Structure of Actin-Binding Proteins

Actin-Associated Proteins and Small Molecules Targeting the Actin Cytoskeleton

An actin cytoskeleton with evolutionarily conserved functions in the absence of canonical actin-binding proteins

Similar Documents

An actin cytoskeleton with evolutionarily conserved functions in the absence of canonical actin-binding proteins.

Evolutionarily conserved surface residues constitute actin binding sites of tropomyosin

A Periodic Pattern of Evolutionarily Conserved Basic and Acidic Residues Constitutes the Binding Interface of Actin-Tropomyosin

An evolutionarily conserved protein binding sequence upstream of a plant light-regulated gene.

Mouse cytoplasmic polyadenylylation element binding protein: An evolutionarily conserved protein that interacts with the cytoplasmic polyadenylylation elements of c-mos mRNA

Controlling the Gate: The Functions of the Cytoskeleton in Stomatal Movement

Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity

Editorial: Evolution, Emerging Functions and Structure of Actin-Binding Proteins

Actin-Associated Proteins and Small Molecules Targeting the Actin Cytoskeleton

An actin cytoskeleton with evolutionarily conserved functions in the absence of canonical actin-binding proteins