A PHP Error was encountered

Severity: Warning

Message: file_get_contents(https://...@pubfacts.com&api_key=b8daa3ad693db53b1410957c26c9a51b4908&a=1): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests

Filename: helpers/my_audit_helper.php

Line Number: 176

Backtrace:

File: /var/www/html/application/helpers/my_audit_helper.php
Line: 176
Function: file_get_contents

File: /var/www/html/application/helpers/my_audit_helper.php
Line: 250
Function: simplexml_load_file_from_url

File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3122
Function: getPubMedXML

File: /var/www/html/application/controllers/Detail.php
Line: 575
Function: pubMedSearch_Global

File: /var/www/html/application/controllers/Detail.php
Line: 489
Function: pubMedGetRelatedKeyword

File: /var/www/html/index.php
Line: 316
Function: require_once

CAMSAP2 localizes to the Golgi in islet β-cells and facilitates Golgi-ER trafficking. | LitMetric

AI Article Synopsis

  • - Glucose stimulation leads to changes in microtubule structures in pancreatic β-cells, which enhances insulin secretion, but knocking down CAMSAP2 reduces insulin levels and affects glucose-stimulated insulin secretion (GSIS) without altering insulin vesicle release.
  • - Instead of stabilizing microtubules at their minus ends like in other cell types, CAMSAP2 primarily localizes to the Golgi apparatus in primary β-cells, which is unique to these cells and does not depend on its ability to bind to microtubules.
  • - The presence of a distinct CAMSAP2 isoform in primary β-cells suggests it has a different role promoting trafficking between the Golgi and endoplasmic reticulum (

Article Abstract

Glucose stimulation induces the remodeling of microtubules, which potentiates insulin secretion in pancreatic β-cells. CAMSAP2 binds to microtubule minus ends to stabilize microtubules in several cultured clonal cells. Here, we report that the knockdown of CAMSAP2 in primary β-cells reduces total insulin content and attenuates GSIS without affecting the releasability of insulin vesicles. Surprisingly, CAMSAP2 knockdown does not change microtubule stability. Unlike in cultured insulinoma cells, CAMSAP2 in primary β-cells predominantly localizes to the Golgi apparatus instead of microtubule minus ends. This novel localization is specific to primary β- but not α-cells and is independent of microtubule binding. Consistent with its specific localization at the Golgi, CAMSAP2 promotes efficient Golgi-ER trafficking in primary β-cells. Moreover, primary β-cells and insulinoma cells likely express different CAMSAP2 isoforms. We propose that a novel CAMSAP2 isoform in primary β-cells has a non-canonical function, which promotes Golgi-ER trafficking to support efficient production of insulin and secretion.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9883185PMC
http://dx.doi.org/10.1016/j.isci.2023.105938DOI Listing

Publication Analysis

Top Keywords

primary β-cells
20
camsap2
8
localizes golgi
8
golgi-er trafficking
8
insulin secretion
8
microtubule minus
8
minus ends
8
camsap2 primary
8
insulinoma cells
8
β-cells
6

Similar Publications

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!