SPRED1 blocking peptide (CDBP6181)

Synthetic SPRED1 blocking peptide for IB

Nature
Synthetic
Immunogen
20 amino acids near the center of human Spred1.
Species Reactivity
Mouse, human, rat
Tag/Conjugate
Unconjugated
Procedure
None
Format
Liquid
Concentration
200 μg/mL
Size
0.05mg
Preservative
None
Storage
-20°C
UniProt ID
Antigen Description
The protein encoded by this gene is a member of the Sprouty family of proteins and is phosphorylated by tyrosine kinase in response to several growth factors. The encoded protein can act as a homodimer or as a heterodimer with SPRED2 to regulate activation of the MAP kinase cascade. Defects in this gene are a cause of neurofibromatosis type 1-like syndrome (NFLS). [provided by RefSeq, Jul 2008]
Function
phosphatase binding; protein binding; protein kinase binding; protein serine/threonine kinase inhibitor activity; stem cell factor receptor binding
Synonyms
SPRED1; sprouty-related, EVH1 domain containing 1; NFLS; hSpred1; spred-1; PPP1R147; sprouty-related, EVH1 domain-containing protein 1; suppressor of Ras/MAPK activation; protein phosphatase 1, regulatory subunit 147

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References


Back to the Future: Proceedings From the 2010 NF Conference

AMERICAN JOURNAL OF MEDICAL GENETICS PART A

Authors: Huson, Susan M.; Acosta, Maria T.; Belzberg, Allan J.; Bernards, Andre; Chernoff, Jonathan; Cichowski, Karen; Evans, D. Gareth; Ferner, Rosalie E.; Giovannini, Marco; Korf, Bruce R.; Listernick, Robert; North, Kathryn N.; Packer, Roger J.; Parada, Luis F.; Peltonen, Juha; Ramesh, Vijaya; Reilly, Karlyne M.; Risner, John W.; Schorry, Elizabeth K.; Upadhyaya, Meena; Viskochil, David H.; Zhu, Yuan; Hunter-Schaedle, Kim; Giancotti, Filippo G.

The neurofibromatoses (NF) encompass the rare diseases NF1, NF2, and schwannomatosis. The NFs affect 100,000 Americans; over 2 million persons worldwide; and are caused by mutation of tumor suppressor genes. Individuals with NF1 in particular may develop tumors anywhere in the nervous system; additional manifestations can include learning disabilities, bone dysplasia, cardiovascular defects, unmanageable pain, and physical disfigurement. Ultimately, the NFs can cause blindness, deafness, severe morbidity, and increased mortality and NF1 includes a risk of malignant cancer. Today there is no treatment for the NFs (other than symptomatic); however, research efforts to understand these genetic conditions have made tremendous strides in the past few years. Progress is being made on all fronts, from discovery studies-understanding the molecular signaling deficits that cause the manifestations of NF-to the growth of preclinical drug screening initiatives and the emergence of a number of clinical trials. An important element in fuelling this progress is the sharing of knowledge, and to this end, for over 20 years the Children's Tumor Foundation has convened an annual NF Conference, bringing together NF professionals to share ideas and build collaborations. The 2010 NF Conference held in Baltimore, MD June 5-8, 2010 hosted over 300 NF researchers and clinicians. This paper provides a synthesis of the highlights presented at the Conference and as such, is a "state-of-the-field" for NF research in 2010. (C) 2010 Wiley-Liss, Inc.

Spred1 and TESK1 - Two new interaction partners of the kinase MARKK/TAO1 that link the microtubule and actin cytoskeleton

MOLECULAR BIOLOGY OF THE CELL

Authors: Johne, Cindy; Matenia, Dorthe; Li, Xiao-yu; Timm, Thomas; Balusamy, Kiruthiga; Mandelkow, Eva-Maria

The signaling from MARKK/TAO1 to the MAP/microtubule affinity-regulating kinase MARK/Par1 to phosphorylated microtubule associated proteins (MAPs) renders microtubules dynamic and plays a role in neurite outgrowth or polarity development. Because hyperphosphorylation of Tau at MARK target sites is a hallmark of Alzheimer neurodegeneration, we searched for upstream regulators by the yeast two-hybrid approach and identified two new interaction partners of MARKK, the regulatory Sprouty-related protein with EVH-1 domain1 (Spred1) and the testis-specific protein kinase (TESK1). Spred1-MARKK binding has no effect on the activity of MARKK; therefore, it does not change microtubule (MT) stability. Spred1-TESK1 binding causes inhibition of TESK1. Because TESK1 can phosphorylate cofilin and thus stabilizes F-actin stress fibers, the inhibition of TESK1 by Spred1 makes F-actin fibers dynamic. A third element in this interaction triangle is that TESK1 binds to and inhibits MARKK. Thus, in Chinese hamster ovary (CHO) cells the elevation of MARKK results in MT disruption (via activation of MARK/Par1 and phosphorylation of MAPs), but this can be blocked by TESK1. Similarly, enhanced TESK1 activity results in increased stress fibers (via phospho-cofilin), but this can be blocked by elevating Spred1. Thus, the three-way interaction between Spred1, MARKK, and TESK1 represents a pathway that links regulation of both the microtubule- and F-actin cytoskeleton.

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