What is furin used for?

Furin is enriched in the Golgi apparatus, where it functions to cleave other proteins into their mature/active forms. Furin cleaves proteins just downstream of a basic amino acid target sequence (canonically, Arg-X-(Arg/Lys) -Arg’).

What does furin cleavage site do?

Furin has a well known role in viral pathogenesis and efficiently cleaves polybasic or multi-basic sites such as those found in influenza virus subtypes H5 and H7. These highly pathogenic avian influenza viruses have therefore served as a model for the role of furin cleavage as a viral virulence factor.

Is furin secreted?

Thus, our results suggest that membrane-bound furin undergoes post-translational processing to produce a soluble form of the enzyme that can be secreted.

Is furin intracellular?

Furin is a cellular endoprotease that was identified in 1990 (BOX 1); it proteolytically activates large numbers of proprotein substrates in secretory pathway compartments. These range from growth factors and receptors to extracellular-matrix proteins and even other protease systems that control disease.

Is furin a membrane protein?

Furin, a ubiquitous membrane protein, is initially produced as a ∼104-kDa precursor and is rapidly converted into an active ∼98-kDa form. This autocatalytic cleavage, occurring in the ER, is a prerequisite for the exit of mature furin molecules from the ER to the TGN and cell surface.

Is furin a serine protease?

Among them, TMPRSS2 and furin play major roles in proteolytic activation of a broad range of viruses (reviewed in references 9, 10, and 11). TMPRSS2 is a type II transmembrane serine protease (TTSP) that is widely expressed in epithelial cells of the respiratory, gastrointestinal, and urogenital tract (11, 12).

Does MERS have a furin cleavage site?

Strikingly, we found that although the R-x-x-R motif at S1/S2 in MERS-CoV has been considered as a furin cleavage site13,14,30, it was cleaved by furin at very low efficiency (Fig. 1d,e).

Is Furin a serine protease?

What class protease is furin?

Abstract. Proteolytic cleavage regulates numerous processes in health and disease. One key player is the ubiquitously expressed serine protease furin, which cleaves a plethora of proteins at polybasic recognition motifs.

What is the structure of furin?

Furin recognizes the R-X-K/R-R motif and cleaves the peptide in the presence of Ca2+ (16,17) and is also known for cleaving different viral (influenza and HIV) envelope glycoproteins, thereby enhancing fusion of the virus with the host cell membrane.

What is SARS 2 spike protein?

It is caused by a novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The spike (S) protein of SARS-CoV-2, which plays a key role in the receptor recognition and cell membrane fusion process, is composed of two subunits, S1 and S2.

What is protein cleavage?

Proteolytic cleavage is basically the process of breaking the peptide bonds between amino acids in proteins. This process is carried out by enzymes called peptidases, proteases or proteolytic cleavage enzymes. Proteins or peptides can be cleaved and used as nutrients.

What is a prohormone convertase also known as?

Prohormone convertases. The two proprotein convertases that specialize in the processing of the precursors of peptide hormones and neuropeptides are also known in the field as “prohormone convertases”. Both “prohormone convertase” and “proprotein convertase” are interchangeably abbreviated as “PC”.

What is the prototypical proprotein convertase?

The prototypical proprotein convertase is furin. Proprotein convertases have medical significance, because they are involved in many important biological processes, such as cholesterol synthesis. Compounds called proprotein convertase inhibitors can block their action, and block the target proteins from becoming active.

Do furin-like proprotein convertases (PPCs) convert 50 kDa HJV to 40 kDa proteins?

Both the Ganz and Rotwein groups demonstrated that furin-like proprotein convertases (PPC) are responsible for conversion of 50 kDa HJV to a 40 kDa protein with a truncated COOH-terminus, at a conserved polybasic RNRR site.

What is the difference between Kex2 and furin?

Kex2 was first purified and characterized by Charles Brenner and Robert Fuller in 1992. The Kex2 crystal structure was solved by a group led by Dagmar Ringe, Robert Fuller and Gregory Petsko. That of Furin was determined by a group led by Manual Than and Wolfram Bode.