Assay and properties of the GIT1/p95-APP1 ARFGAP.

Methods Enzymol

San Rafaele Scientific Institute, Department of Molecular Biology and Functional Genomics, Milano, Italy.

Published: March 2006

GIT1/p95-APP1 is an adaptor protein with an aminoterminal ARFGAP domain involved in the regulation of ARF6 function. GIT1/p95-APP1 forms stable complexes with a number of proteins including downstream effectors and exchanging factors for members of the Rho family of small GTPases. This protein can also interact with other adaptor proteins implicated in the regulation of cell adhesion and synapse formation. The stability of the endogenous and reconstituted complexes after cell lysis allows the biochemical identification and characterization of the GIT1 complexes that can be isolated from different cell types. This article presents methods for the identification of the endogenous and reconstituted GIT1 complexes that can be utilized for the biochemical and functional characterization of the complexes from different tissue and cell types.

Download full-text PDF

Source
http://dx.doi.org/10.1016/S0076-6879(05)04025-5DOI Listing

Publication Analysis

Top Keywords

endogenous reconstituted
8
git1 complexes
8
cell types
8
complexes
5
assay properties
4
properties git1/p95-app1
4
git1/p95-app1 arfgap
4
arfgap git1/p95-app1
4
git1/p95-app1 adaptor
4
adaptor protein
4

Similar Publications

Background: The adoptive cell transfer (ACT) of T cell receptor (TCR)-engineered T cells targeting the HLA-A2-restricted epitope NY-ESO-1 (A2/NY) has yielded important clinical responses against several cancers. A variety of approaches are being taken to augment tumor control by ACT including TCR affinity-optimization and T-cell coengineering strategies to address the suppressive tumor microenvironment (TME). Most TCRs of clinical interest are evaluated in immunocompromised mice to enable human T-cell engraftment and do not recapitulate the dynamic interplay that occurs with endogenous immunity in a treated patient.

View Article and Find Full Text PDF

Biomimetic nanostructural materials based on placental amniotic membrane-derived nanofibers for self-healing and anti-adhesion during cesarean section.

Biomaterials

January 2025

Translational Medicine Research Center, Zhujiang Hospital, Southern Medical University, Guangzhou, 510280, China; Greater Bay Area Institute of Precision Medicine (Guangzhou), Fudan University, Guangzhou, 511462, China. Electronic address:

Cesarean section (CS) is highly prevalent surgery among females. However, current absorbable anti-adhesion membranes used clinically can partially prevent postoperative adhesions but show limited efficacy in tissue regeneration, leaving post-cesarean women at risk for severe complications including cesarean scar pregnancy, placenta previa, and uterine rupture. Herein, we designed a fully amniotic membrane (AM)-derived biomimetic nanostructural materials (AM-BNMs) as an anti-adhesion barrier, and validated its therapeutic efficacy in a rat CS model.

View Article and Find Full Text PDF

Reconstituting the immune killing functions and improving the pharmacokinetics of nanobodies by rhamnolipid conjugation.

J Control Release

December 2024

Key Laboratory of Carbohydrate Chemistry & Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, China. Electronic address:

Nanobodies (Nbs) hold great promise as next-generation cancer immunotherapies, but their efficacy is hindered by their poor pharmacokinetics and the inability to trigger Fc-mediated immune killing functions. To address these limitations, we designed and synthesized rhamnolipid-modified Nbs as a type of antibody-recruiting molecule by site-specifically conjugating EGFR-targeting Nb 7D12 to a series of rhamnolipid derivatives, and their biological profiles were evaluated in vitro and in vivo. Investigation of the structure-activity relationship revealed that the number of rhamnose (Rha) units and the length of the PEG linker in the conjugates affected anti-tumor activities.

View Article and Find Full Text PDF

Protein aggregation behavior during highland barley dough formation induced by different hordein/glutelin ratio.

Food Chem

February 2025

Beijing Key Laboratory of Bioactive Substances and Functional Foods, Beijing Union University, Beijing, 100023, PR China. Electronic address:

Article Synopsis
  • The study focused on understanding why highland barley dough lacks a gluten structure by examining how the hordein/glutelin protein ratio affects dough properties.
  • Findings revealed that a balanced ratio (50Hordein-50Glutelin) led to improved dough quality by enhancing protein crosslinking and network structure.
  • The research highlights the potential for improving barley and similar grain products' quality through adjustments in their protein composition.
View Article and Find Full Text PDF

Liver diseases are one of the leading causes of morbidity and mortality worldwide. Globally, liver diseases are responsible for approximately 2 million deaths annually (1 of every 25 deaths). Many of the patients with chronic liver diseases can benefit from organ transplantation.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!