[7] Cellulose is an aggregation of unbranched polymer chains made of β-(1→4)-linked glucose residues that makes up a large portion of primary and secondary cell walls.

[7][6][12][13] Worldwide, 2 × 1011 tons of cellulose microfibrils are produced,[14] which serves as a critical source of renewable biofuels and other biological-based products, such as lumber, fuel, fodder, paper and cotton.

Solution x-ray scattering have shown that CesAs are at the surface of a plant cell and are elongated monomers with a two catalytic domains that fuse together into dimers.

[9][12] The broader of the two structures (Sethaphong 2013), which includes the entire middle cytoplasmic domain (again sandwiched between TM helices), gives a useful view of the enzyme: two plant-specific insertions called the PC-R (plant-conserved region, similar in all plants) on the N-terminal end and CS-R (class-specific region, determines the subclass number after CesA) on the C-terminal end punctuate the usual GT catalytic core, probably providing the unique rosette-forming function of plant CesA.

[12] A 2016 experimental model of the PC-R (5JNP) domain helps to fill in this gap, as it greatly improves the fit against Olek's previous result.

[9] Cellulose biosynthesis is the process during which separate homogeneous β-(1→4)-glucan chains, ranging from 2,000 to 25,000 glucose residues in length, are synthesized and then immediately hydrogen bond with one another to form rigid crystalline arrays, or microfibrils.

[26][27] Microfibril synthesis is guided by cortical microtubules, which lie beneath the plasma membrane of elongating cells, in that they form a platform on which the CSCs can convert glucose molecules into the crystalline chains.

The microtubule–microfibril alignment hypothesis proposes that cortical microtubules, which lie beneath the plasma membrane of elongating cells, provide tracks for CSCs that convert glucose molecules into crystalline cellulose microfibrils.

[25] Additionally, the KORRIGAN (KOR1) protein is thought to be a critical component of cellulose synthesis in that it acts as a cellulase at the plasma membrane-cell wall interface.

KOR1 interacts with a two specific CesA proteins, possibly by proof-reading and relieving stress created by glucan chain synthesis, by hydrolyzing disordered amorphous cellulose.

Interactions with these factors may influence cellulose deposition in that it affects the amount of substrate produced and the concentration and/or activity of CSCs in the plasma membrane.