alexa Identification And Functional Evaluation Of LRIG1-interacting Proteins
ISSN: 1948-5956

Journal of Cancer Science & Therapy
Open Access

Like us on:
OMICS International organises 3000+ Global Conferenceseries Events every year across USA, Europe & Asia with support from 1000 more scientific Societies and Publishes 700+ Open Access Journals which contains over 50000 eminent personalities, reputed scientists as editorial board members.

Open Access Journals gaining more Readers and Citations

700 Journals and 15,000,000 Readers Each Journal is getting 25,000+ Readers

This Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)

Share This Page

Additional Info

Loading Please wait..

JOINT EVENT:19th Euro Congress on Cancer Science and Therapy & 25th Cancer Nursing & Nurse Practitioners Conference
July 17-19, 2017 Lisbon, Portugal

Mahmood Faraz
Umea University, Sweden
ScientificTracks Abstracts: J Cancer Sci Ther
DOI: 10.4172/1948-5956-C1-105
Leucine-rich repeats and immunoglobulin-like domains 1 (LRIG1) is a tumor suppressor and a negative regulator of different receptor tyrosine kinases (RTKs). The molecular mechanisms whereby LRIG1 mediates tumor suppression and regulates RTKs remain incompletely understood. Here, we performed a yeast two-hybrid screen to identify novel LRIG1-interacting proteins and datamined the BioPlex protein interaction data repository. All the putative LRIG1-interactors identified were functionally evaluated in a triple co-transfection system where HEK293 cells were co-transfected with platelet-derived growth factor receptor alpha (PDGFRA) and LRIG1 together with shRNAs against the identified LRIG1-interactors.We took advantage of the ability of LRIG1 to downregulate the PDGFRA expression levels and evaluated the effects of the shRNAs against different LRIG1-interactors on the resulting PDGFRA levels. Based on the protein interaction data and our functional results, we propose a functional LRIG1 protein interaction network that contained mostly novel and unanticipated components. The network contained the functionally important LRIG1- interacting proteins RAB4A, PON2, GLRX3, GAL3ST1, TUBB8, ZBTB16, LRIG2, CNPY3, HLA-DRA, GML, CNPY4, LRRC40, and LRIG3, together with PTPRK and other proteins. In silico analyses of the cancer genome atlas (TCGA) data sets revealed consistent correlations between the expression of the transcripts for LRIG1 and its inter-actors ZBTB16 and PTPRK, and inverse correlations between the transcripts for LRIG1 and GLRX3. PON2 was further experimentally studied and found to co-localize with LRIG1 in LRIG1 transfected cells. We suggest that the proposed LRIG1 protein interaction network will provide important novel leads for future studies aiming at understanding the molecular functions of LRIG1 and its tumor suppressive functions.

Mahmood Faraz is a PhD student in Umea University, Sweden.

Email: [email protected]

image PDF   |   image HTML

Relevant Topics

Peer Reviewed Journals
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version